Superoxide Dismutase 1, Soluble Proteine (SOD1)

Superoxide Dismutase 1, Soluble Proteine (SOD1)
Auf finden Sie aktuell 108 Superoxide Dismutase 1, Soluble (SOD1) Proteine von 18 unterschiedlichen Herstellern. Zusätzlich bieten wir Ihnen Superoxide Dismutase 1, Soluble Antikörper (532) und Superoxide Dismutase 1, Soluble Kits (82) und viele weitere Produktgruppen zu diesem Protein an. Insgesamt sind aktuell 737 Superoxide Dismutase 1, Soluble Produkte verfügbar.
Albs, als, als1, B430204E11Rik, CG11793, cSod, Cu, Cu-Zn SOD, CU/ZN-SOD, Cu/ZnSOD, Cu/Zn sod, Cu/Zn superoxide dismutase, CuSOD, cuzn, CuZn-SOD, CuZn-SOD1, CuZnSOD, CuZn SOD, Cu[2+]/Zn[2+]SOD, DKFZP469M1833, Dmel\\CG11793, dSOD1, G, homodimer, hSod1, Ipo-1, Ipo1, ipoa, l(3)68Af', l(3)108, l(3)G, LOC692639, mKIAA4111, Mn SOD, sod, Sod-1, Sod1, sod1-a, SOD1L1, SODC, To, To-1, XSODB, Zn-SOD, ZnSod, Zn Sod, ZSOD
alle Proteine anzeigen Gen GeneID UniProt
Maus SOD1 SOD1 16005 P70389
Ratte SOD1 SOD1 79438 P35859
Human SOD1 SOD1 6647 P00441

Weitere Synonyme anzeigen

Superoxide Dismutase 1, Soluble Proteine (SOD1) nach Spezies

Wählen Sie die gewünschte Spezies

Am meisten referenzierte Superoxide Dismutase 1, Soluble Proteine

  1. Human SOD1 Protein expressed in Escherichia coli (E. coli) - ABIN2004728 : Kostrzewa, Damian, Müller: Superoxide dismutase 1: identification of a novel mutation in a case of familial amyotrophic lateral sclerosis. in Human genetics 1996 (PubMed)
    Zeige alle 4 Referenzen für 2004728

  2. Human SOD1 Protein expressed in Escherichia coli (E. coli) - ABIN667079 : Banci, Bertini, Boca, Girotto, Martinelli, Valentine, Vieru: SOD1 and amyotrophic lateral sclerosis: mutations and oligomerization. in PLoS ONE 2008 (PubMed)
    Zeige alle 3 Referenzen für 667079

Weitere Proteine zu Superoxide Dismutase 1, Soluble Interaktionspartnern

Silk Worm Superoxide Dismutase 1, Soluble (SOD1) Interaktionspartner

Mouse (Murine) Superoxide Dismutase 1, Soluble (SOD1) Interaktionspartner

  1. 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

  2. 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.

  3. the aberrant mutant SOD1-G3BP1 (zeige G3BP1 Proteine) interaction affects stress granule dynamics

  4. 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.

  5. the redox regulation of Jmjd3 is a unique regulatory mechanism for Cu,Zn-superoxide dismutase-mediated profibrotic macrophage polarization.

  6. two ALS-linked factors, SQSTM1 (zeige SQSTM1 Proteine) and ALS2, have distinct but additive protective roles against mutant SOD1-mediated toxicity by modulating neuronal proteostasis possibly through the autophagy-endolysosomal system.

  7. we showed that, in the absence of ERalpha (zeige ESR1 Proteine), G93A-SOD1 failed to activate OMI (zeige HTRA2 Proteine) and the proteasome, confirming the ERalpha (zeige ESR1 Proteine) 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

  8. 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 (zeige ELN Proteine). We conclude that superoxide is a driver of both cerebral vascular hypertrophy and vasomotor dysfunction in a model of hyperhomocysteinemia.

  9. SOD1 has a role in amyotrophic lateral sclerosis disease phenotype

  10. the damage and satellite cell state of the gastrocnemius muscle in SOD1 knockout mice, was investigated.

Caenorhabditis elegans (C. elegans) Superoxide Dismutase 1, Soluble (SOD1) Interaktionspartner

  1. the C. elegans intracellular CuZn-SODs (wSOD-1 and wSOD-5) are not dependent on the copper chaperone CCS (zeige CCS Proteine) for activation

  2. although several long-lived mutants of Caenorhabditis elegans have increased SOD levels, this phenomenon does not correlate with life span or growth rate.

  3. 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.

  4. the ALS-linked mutant SOD1 produces a locomotor defect associated with aggregation and synaptic dysfunction when expressed in neurons of Caenorhabditis elegans

  5. 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.

Fruit Fly (Drosophila melanogaster) Superoxide Dismutase 1, Soluble (SOD1) Interaktionspartner

  1. The functional SOD1 and SOD2 (zeige SOD2 Proteine) genes knockout and their overexpression in neurons and glial tissue increase the sensitivity of Drosophila melanogaster to oxidative stress conditions.

  2. Expression of zinc-deficient human superoxide dismutase (zeige SOD2 Proteine) in Drosophila neurons produces a locomotor defect linked to mitochondrial dysfunction.

  3. curcumin increases mean lifespan of Drosophila via regulating gene expression of the key enzyme SOD and reducing accumulation of MDA and lipid peroxidation.

  4. 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.

  5. Overexpression of Cu,ZnSOD and MnSOD (zeige SOD2 Proteine) in transgenic Drosophila.

  6. Effects of overexpression of copper-zinc and manganese superoxide dismutases, catalase, and thioredoxin reductase genes on longevity.

  7. SOD1 and SOD2 (zeige SOD2 Proteine) provide independent protection to compartment-specific protein iron-sulfur clusters against attack by superoxide generated under oxidative stress

  8. 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.

  9. Cu/Zn superoxide dismutase has a role in preventing spontaneous DNA damage

  10. Instability of superoxide dismutase 1 of Drosophila in mutants deficient for its cognate copper chaperone

Human Superoxide Dismutase 1, Soluble (SOD1) Interaktionspartner

  1. 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

  2. Factors released in vitro from astrocytes derived from SOD-1 transgenic mice cause spinal motoneuron death and consequent neuromuscular dysfunction in vivo.

  3. This study identified a new pathology hallmark in SOD1G93A ALS mice: a glutamatergic sensory neuron dendropathy restricted to olfactory bulb mitral cells and retinal ganglionic cells.

  4. demonstrated that enervating the SOD1 electrostatic loop can lead to an experimentally observed gain of interaction (GOI) responsible for the formation of SOD1 amyloid-like filaments

  5. Sod1 upregulation was noted in the R region of the nonaneurysmal type 1 L/R morphotype. Region-specific transcription profiles of Sod on the basis of BAV morphotype deepen our understanding of its associated aortopathy and provide biological insight on the asymmetric dilatation pattern.

  6. This study demonstrated that the injection into isolated Aplysia neurons of oligomeric forms of a mutant G85R SOD1 associated with ALS in both humans and transgenic mice reduces net outward K+ current and increases excitability.

  7. sodium channel currents in oocytes expressing either wild-type or mutant (A4V) SOD1 protein

  8. findings indicate that CuZn-SOD is able to response to the hypomagnetic field stress and suggest it a mediator of the hypomagnetic field effect.

  9. Data suggest that Ccs1 activates immature Sod1 by delivering copper and facilitating oxidation of intramolecular disulfide bond in Sod1; Ccs1 binding exposes an electropositive cavity and proposed "entry site" for copper ion delivery on the apoenzyme. (Ccs1 = copper chaperone for superoxide dismutase (zeige CCS Proteine); Sod1 = copper-zinc superoxide dismutase)

  10. The cause of aggregation and reduced Zn binding affinity by G85R mutation in SOD1 rendering amyotrophic lateral sclerosis has been described.

Pig (Porcine) Superoxide Dismutase 1, Soluble (SOD1) Interaktionspartner

  1. 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

Cow (Bovine) Superoxide Dismutase 1, Soluble (SOD1) Interaktionspartner

  1. SOD catalyzes reversal of autoxidation manifesting as its inhibition. SOD saves catechols from autoxidation and extends their bioavailability

  2. antioxidative enzymatic mechanisms in bovine placental tissues are represented by superoxide dismutase 1 and glutathione peroxidase (zeige GPX1 Proteine), which show the changes in their expression during improper placental release

  3. 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.

  4. ALOX5AP (zeige ALOX5AP Proteine), CPNE3 (zeige CPNE3 Proteine), IL1R2 (zeige IL1R2 Proteine), IL6 (zeige IL6 Proteine), TLR2, TLR4 (zeige TLR4 Proteine), and THY1 (zeige THY1 Proteine) were upregulated in blood polymorphonuclear cells in negative energy balance versus positive energy balance cows.

  5. Acute elevation of SOD may represent a response of luteal endothelial cells to protect themselves against oxidative stress induced (zeige SQSTM1 Proteine) by PGF (zeige PGF Proteine) during functional luteolysis.

  6. 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 (zeige CAT Proteine).

  7. 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 (zeige C9orf3 Proteine)-monomer SOD-1 was calculated.

  8. 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 (zeige GYPA Proteine). The crystal structure (hpSOD) was determined and refined at 2 A degrees resolution.

  9. 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)

  10. Bovine erythrocyte Cu,Zn-superoxide dismutase (BESOD) is a dimeric enzyme composed of identical subunits associated through unusually strong non-covalent interactions.

Rabbit Superoxide Dismutase 1, Soluble (SOD1) Interaktionspartner

  1. 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.

Zebrafish Superoxide Dismutase 1, Soluble (SOD1) Interaktionspartner

  1. 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 (zeige CAT Proteine) and superoxide dismutase (SOD)-1.

  2. 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.

  3. A hierarchic gene expression of copper homeostatic genes was demonstrated between atp7a (zeige ATP7A Proteine), sp1 (zeige SP1 Proteine) and sod1 in zebrafish.

  4. depresses cathepsin L (zeige CTSL1 Proteine) activity stimulated by free radicals and prevents otic complications associated with bone erosion

  5. Copper/zinc superoxide dismutase was cloned from the zebrafish ( Danio rerio). Evidence is presented that SOD protects against paraquat toxicity in fish.

  6. Glia maturation factor-null cells ahow a concurrent decrease in CuZnSOD astrocytes.

Superoxide Dismutase 1, Soluble (SOD1) Protein Überblick

Protein Überblick

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.

Alternative names and synonyms associated with Superoxide Dismutase 1, Soluble (SOD1)

  • superoxide dismutase 1, soluble (sod1)
  • Superoxide dismutase [Cu-Zn] (SOD1)
  • Cu/Zn superoxide dismutase (A245R)
  • Cu/Zn superoxide dismutase (SOD2.2)
  • Cu/Zn superoxide dismutase (sod1)
  • superoxide dismutase 1, soluble (SOD1)
  • Cu/Zn superoxide dismutase (SOD)
  • insulin-like growth factor binding protein, acid labile subunit (Igfals)
  • Protein SOD-1 (sod-1)
  • Superoxide dismutase (Sod)
  • superoxide dismutase [Cu-Zn]-like (LOC101451855)
  • superoxide dismutase 1, soluble (Sod1)
  • superoxide dismutase 1, soluble (sod1-b)
  • Albs Protein
  • als Protein
  • als1 Protein
  • B430204E11Rik Protein
  • CG11793 Protein
  • cSod Protein
  • Cu Protein
  • Cu-Zn SOD Protein
  • CU/ZN-SOD Protein
  • Cu/ZnSOD Protein
  • Cu/Zn sod Protein
  • Cu/Zn superoxide dismutase Protein
  • CuSOD Protein
  • cuzn Protein
  • CuZn-SOD Protein
  • CuZn-SOD1 Protein
  • CuZnSOD Protein
  • CuZn SOD Protein
  • Cu[2+]/Zn[2+]SOD Protein
  • DKFZP469M1833 Protein
  • Dmel\\CG11793 Protein
  • dSOD1 Protein
  • G Protein
  • homodimer Protein
  • hSod1 Protein
  • Ipo-1 Protein
  • Ipo1 Protein
  • ipoa Protein
  • l(3)68Af' Protein
  • l(3)108 Protein
  • l(3)G Protein
  • LOC692639 Protein
  • mKIAA4111 Protein
  • Mn SOD Protein
  • sod Protein
  • Sod-1 Protein
  • Sod1 Protein
  • sod1-a Protein
  • SOD1L1 Protein
  • SODC Protein
  • To Protein
  • To-1 Protein
  • XSODB Protein
  • Zn-SOD Protein
  • ZnSod Protein
  • Zn Sod Protein
  • ZSOD Protein

Bezeichner auf Proteinebene für SOD1

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 , CG11793-PA , CG11793-PD , Cu, Zn superoxide dismutase , Cu-Zn superoxide dismutase , Cu/Zn-Superoxide dismutase , CuZn superoxide dismutase , CuZn-superoxide dismutase , CuZn-superoxide dismutase (SOD)1 , CuZnSOD , Cu[2+] Zn[2+] superoxide dismutase , Cu[2+]Zn[2+] superoxide dismutase , Mn superoxide dismutase , Sod-PA , Sod-PD , complementation group G , copper and zinc SOD , copper-zinc superoxide , copper-zinc superoxide dismutase , cytoplasmic Cu/ZnSOD , dismutase , super oxide dismutase , superoxidase dismutase , superoxide dismutase 1 , superoxide dismutatase , superoxide-dismutase , 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 , sod(Cu/Zn) , Cu,Zn superoxide dismutase , superoxide dismutase [Cu-Zn] B

100381040 Xenopus laevis
100499991 Glycine max
918416 Paramecium bursaria Chlorella virus 1
4836692 Scheffersomyces stipitis CBS 6054
100136454 Salmo salar
100172349 Pongo abelii
692639 Bombyx mori
16005 Mus musculus
79438 Rattus norvegicus
174141 Caenorhabditis elegans
39251 Drosophila melanogaster
101451855 Ceratitis capitata
6647 Homo sapiens
20655 Mus musculus
24786 Rattus norvegicus
100033855 Equus caballus
100135622 Cavia porcellus
403559 Canis lupus familiaris
397036 Sus scrofa
281495 Bos taurus
101115136 Ovis aries
100009313 Oryctolagus cuniculus
395938 Gallus gallus
100270717 Ovis aries
449637 Pan troglodytes
100861196 Capra hircus
574096 Macaca mulatta
30553 Danio rerio
394274 Xenopus laevis
Ausgewählte Anbieter für Superoxide Dismutase 1, Soluble Proteine (SOD1)
Haben Sie etwas anderes gesucht?