| Name | SOD1 |
|---|---|
| Synonyms | ALS; ALS 1; ALS1; IPOA; Indophenoloxidase A; SOD; SOD 1; SOD1… |
| Name | paraquat |
|---|---|
| CAS | 1,1′-dimethyl-4,4′-bipyridinium |
| PubMed | Abstract | RScore(About this table) | |
|---|---|---|---|
| 19059428 | Yen K, Patel HB, Lublin AL, Mobbs CV: 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. Mech Ageing Dev. 2009 Mar;130(3):173-8. Epub 2008 Nov 19. We find no significant decrease in lifespan for control worms or worms undergoing DR when sod isoforms are knocked-out even though sod mutational inactivation produces hypersensitivity to paraquat. In contrast, sod-1 inactivation significantly reduces lifespan extension by CHIL, suggesting that CHIL requires a specific genetic program beyond simple reduction in metabolic rate. |
1(0,0,0,1) | Details |
| 12456885 | Kirby K, Hu J, Hilliker AJ, Phillips JP: RNA interference-mediated silencing of Sod2 in Drosophila leads to early adult-onset mortality and elevated endogenous oxidative stress. Proc Natl Acad Sci U S A. 2002 Dec 10;99(25):16162-7. Epub 2002 Nov 27. Although genetic studies with mutants deficient in SOD1, the predominantly cytosolic isoform of SOD, have been instrumental in elucidating the role of reactive metabolism in aging in Drosophila, the lack of available mutations in the Sod2 gene has hampered an equivalent analysis of the participation of this important antioxidant enzyme in the Drosophila aging model. |
1(0,0,0,1) | Details |
| 18073424 | Yang W, Li J, Hekimi S: A Measurable increase in oxidative damage due to reduction in detoxification fails to shorten the life span of long-lived mitochondrial mutants of Caenorhabditis elegans. Genetics. 2007 Dec;177(4):2063-74. Furthermore, although disruption of sod-1 or -2 expression produces numerous phenotypes, including increased sensitivity to paraquat and increased oxidative damage to proteins (except in daf-2 mutants), this fails to shorten the life span of these long-lived mutants. In fact, sod-1 (RNAi) increases the life span of daf-2 mutants and sod-2 (RNAi) that of clk-1 mutants. |
1(0,0,0,1) | Details |
| 12972424 | Missirlis F, Hu J, Kirby K, Hilliker AJ, Rouault TA, Phillips JP: Compartment-specific protection of iron- proteins by superoxide dismutase. J Biol Chem. 2003 Nov 28;278(48):47365-9. Epub 2003 Sep 12. We also find that exposure of adults to paraquat converts cytosolic aconitase to IRP1 but has no affect on mitochondrial aconitase, indicating that paraquat generates in the cytosol but not in mitochondria. |
0(0,0,0,0) | Details |
| 16184763 | Batulan Z, Nalbantoglu J, Durham HD: Nonsteroidal anti-inflammatory drugs differentially affect the heat shock response in cultured spinal cord cells. Cell Stress Chaperones. 2005 Autumn;10(3):185-96. At concentrations that increased Hsp70 in heat shocked glial cells, failed to delay death of motor neurons exposed to hyperthermia, paraquat-mediated oxidative stress, and excitotoxicity. |
0(0,0,0,0) | Details |
| 15965076 | Chou CM, Huang CJ, Shih CM, Chen YP, Liu TP, Chen CT: Identification of three mutations in the Cu,Zn-superoxide dismutase (Cu,Zn-SOD) gene with familial amyotrophic lateral sclerosis: transduction of human Cu,Zn-SOD into PC12 cells by HIV-1 TAT protein basic domain. Ann N Y Acad Sci. 2005 May;1042:303-13. In undifferentiated PC12 cells, wild-type Tat-SOD1 could prevent DNA fragmentation due to attacks generated by 35 mM paraquat, whereas mutant Tat-D101G enhanced cell death. |
88(1,1,1,8) | Details |
| 10694572 | Wong PC, Waggoner D, Subramaniam JR, Tessarollo L, Bartnikas TB, Culotta VC, Price DL, Rothstein J, Gitlin JD: Copper chaperone for superoxide dismutase is essential to activate mammalian Cu/Zn superoxide dismutase. Proc Natl Acad Sci U S A. 2000 Mar 14;97(6):2886-91. Consistent with this loss of SOD1 activity, CCS (-/-) mice showed increased sensitivity to paraquat and reduced female fertility, phenotypes that are characteristic of SOD1-deficient mice. |
83(1,1,1,3) | Details |
| 19135146 | James BP, Staatz WD, Wilkinson ST, Meuillet E, Powis G: Superoxide dismutase is regulated by LAMMER kinase in Drosophila and human cells. Free Radic Biol Med. 2009 Mar 15;46(6):821-7. Epub 2008 Dec 24. We have shown that mutations in the Drosophila LAMMER kinase gene, Darkener of apricot (Doa), protect against the decrease in life span caused by the reactive species (ROS) generator paraquat, and at the same time show an increase in cytoplasmic (CuZn-Sod or SOD1) and mitochondrial superoxide dismutase (Mn-Sod or SOD2) protein levels and activity. |
34(0,1,1,4) | Details |
| 18725537 | Medicherla B, Goldberg AL: Heat shock and radicals stimulate ubiquitin-dependent degradation mainly of newly synthesized proteins. J Cell Biol. 2008 Aug 25;182(4):663-73. However, exposure to 38 degrees C, paraquat, cadmium, or deletion of SOD1 enhanced two- to threefold the degradation of newly synthesized proteins. |
31(0,1,1,1) | Details |
| 16677106 | Mele J, Van Remmen H, Vijg J, Richardson A: Characterization of transgenic mice that overexpress both zinc superoxide dismutase and catalase. Antioxid Redox Signal. 2006 Mar-Apr;8(3-4):628-38. The murine embryonic fibroblasts (MEFs) from the Tg (SOD1/CAT) +/o and MEFs overexpressing Cu/ZnSOD were more resistant to paraquat cytotoxicity, relative to wild-type MEFs. |
14(0,0,2,4) | Details |
| 11590119 | Oeda T, Shimohama S, Kitagawa N, Kohno R, Imura T, Shibasaki H, Ishii N: Oxidative stress causes abnormal accumulation of familial amyotrophic lateral sclerosis-related mutant SOD1 in transgenic Caenorhabditis elegans. Hum Mol Genet. 2001 Sep 15;10(19):2013-23. The transgenic strains expressing mutant human SOD1 showed greater vulnerability to oxidative stress induced by 0.2 mM paraquat than a control that contained the wild-type human SOD1. |
12(0,0,1,7) | Details |
| 10446154 | Yoo HY, Chang MS, Rho HM: The activation of the rat /zinc superoxide dismutase gene by peroxide through the peroxide-responsive element and by paraquat and heat shock through the same heat shock element. J Biol Chem. 1999 Aug 20;274(34):23887-92. The promoter activity of the SOD1 gene was increased 3-5-fold by peroxide, paraquat (PQ) and heat shock. |
11(0,0,1,6) | Details |
| 15034941 | Turner BJ, Lopes EC, Cheema SS: Inducible superoxide dismutase 1 aggregation in transgenic amyotrophic lateral sclerosis mouse fibroblasts. J Cell Biochem. 2004 Apr 1;91(5):1074-84. In contrast, paraquat-mediated stress in fibroblasts promoted aggregation of endogenous SOD1, but not mutant SOD1. |
10(0,0,0,10) | Details |
| 17324120 | Agbas A, Hui D, Wang X, Tek V, Zaidi A, Michaelis EK: Activation of brain calcineurin (Cn) by Cu-Zn superoxide dismutase (SOD1) depends on direct SOD1-Cn protein interactions occurring in vitro and in vivo. Biochem J. 2007 Jul 1;405(1):51-9. |
10(0,0,0,10) | Details |
| 16730205 | Choi YS, Lee KS, Yoon HJ, Kim I, Sohn HD, Jin BR: Bombus ignitus Cu,Zn superoxide dismutase (SOD1): cDNA cloning, gene structure, and up-regulation in response to paraquat, temperature stress, or lipopolysaccharide stimulation. Comp Biochem Physiol B Biochem Mol Biol. 2006 Jul;144(3):365-71. Epub 2006 Apr 7. |
10(0,0,1,5) | Details |
| 16741961 | Dong A, Shen J, Krause M, Akiyama H, Hackett SF, Lai H, Campochiaro PA: Superoxide dismutase 1 protects retinal cells from oxidative damage. J Cell Physiol. 2006 Sep;208(3):516-26. These data demonstrate that SOD1 protects retinal cells against paraquat- and hyperoxia-induced oxidative damage and suggest that overexpression of SOD1 should be considered as one component of ocular gene therapy to prevent oxidative damage-induced retinal degeneration. |
8(0,0,1,3) | Details |
| 11581253 | Wei JP, Srinivasan C, Han H, Valentine JS, Gralla EB: Evidence for a novel role of -zinc superoxide dismutase in zinc metabolism. J Biol Chem. 2001 Nov 30;276(48):44798-803. Epub 2001 Oct 1. The LYS7 gene in Saccharomyces cerevisiae encodes a protein (yCCS) that delivers to the active site of -zinc superoxide dismutase (CuZn-SOD, a product of the SOD1 gene). Here, we demonstrate certain phenotypic differences between these strains: 1) lys7Delta cells are slightly less sensitive to paraquat than sod1Delta cells, 2) EPR-detectable or "free" iron is dramatically elevated in sod1Delta mutants but not in lys7Delta yeast, and 3) although sod1Delta mutants show increased sensitivity to extracellular zinc, the lys7Delta strain is as resistant as wild type. |
3(0,0,0,3) | Details |
| 14598305 | Turner BJ, Rembach A, Spark R, Lopes EC, Cheema SS: Opposing effects of low and high-dose clozapine on survival of transgenic amyotrophic lateral sclerosis mice. J Neurosci Res. 2003 Nov 15;74(4):605-13. Aside from well-described and serotonin receptor blockade effects, clozapine may also be neuroprotective through its modulation of the p75 neurotrophin receptor (p75 (NTR)) and superoxide dismutase 1 (SOD1) expression. Furthermore, low concentrations of clozapine protected NSC-34 cells from paraquat-mediated toxicity, nerve growth factor (NGF)-induced death signalling, and serum deprivation, whereas high concentrations potentiated death. |
3(0,0,0,3) | Details |
| 20039174 | Fischer LR, Glass JD: Oxidative stress induced by loss of Cu,Zn-superoxide dismutase (SOD1) or -generating herbicides causes axonal degeneration in mouse DRG cultures. Acta Neuropathol. 2010 Feb;119(2):249-59. Epub 2009 Dec 29. To test susceptibility to increased production, we exposed wild-type DRGs to the redox-cycling herbicides paraquat and diquat (DQ). |
5(0,0,0,5) | Details |
| 19332122 | Turner BJ, Parkinson NJ, Davies KE, Talbot K: Survival motor neuron deficiency enhances progression in an amyotrophic lateral sclerosis mouse model. Neurobiol Dis. 2009 Jun;34(3):511-7. Epub 2009 Mar 28. Mutations in the ubiquitously expressed survival motor neuron 1 (SMN1) and superoxide dismutase 1 (SOD1) genes are selectively lethal to motor neurons in spinal muscular atrophy (SMA) and familial amyotrophic lateral sclerosis (ALS), respectively. Treatment with the environmental toxin paraquat also depleted SMN protein, implicating oxidative stress in the mechanism underlying SMN deficiency in familial ALS and potentially sporadic disease. |
5(0,0,0,5) | Details |
| 15288509 | Taylor DM, Minotti S, Agar JN, Durham HD: Overexpression of metallothionein protects cultured motor neurons against oxidative stress, but not mutant Cu/Zn-superoxide dismutase toxicity. Neurotoxicology. 2004 Sep;25(5):779-92. Mutations in Cu/Zn-superoxide dismutase 1 (SOD1) are responsible for a familial form of amyotrophic lateral sclerosis (FALS). MT-III expression was restricted to neurons and was unaffected by treatment with ZnCl (2), paraquat, or |
3(0,0,0,3) | Details |
| 18319614 | An JJ, Lee YP, Kim SY, Lee SH, Kim DW, Lee MJ, Jeong MS, Jang SH, Kang JH, Kwon HY, Kang TC, Won MH, Cho SW, Kwon OS, Lee KS, Park J, Eum WS, Choi SY: Transduction of familial amyotrophic lateral sclerosis-related mutant PEP-1-SOD proteins into neuronal cells. Mol Cells. 2008 Feb 29;25(1):55-63. Mutations in the SOD1 gene are responsible for a familial form of ALS (FALS). Neurones harboring the A4V, G93A, G85R, and D90A mutants of PEP-1-SOD were more vulnerable to oxidative stress induced by paraquat than those harboring wild-type proteins. |
3(0,0,0,3) | Details |
| 19129474 | Tan SX, Teo M, Lam YT, Dawes IW, Perrone GG: Cu, Zn superoxide dismutase and (H) homeostasis are required for tolerance of endoplasmic reticulum stress in Saccharomyces cerevisiae. Mol Biol Cell. 2009 Mar;20(5):1493-508. Epub 2009 Jan 7. Genome-wide screening for sensitivity to chronic endoplasmic reticulum (ER) stress induced by and tunicamycin (TM) identified mutants deleted for Cu, Zn superoxide dismutase (SOD) function (SOD1, CCS1) or affected in generation via the pentose phosphate pathway (TKL1, RPE1). Prior adaptation of the hac1 mutant deficient in the unfolded protein response (UPR) to the -generating agent paraquat reduced cell death under ER stress. |
3(0,0,0,3) | Details |
| 12470895 | Yanase S, Yasuda K, Ishii N: Adaptive responses to oxidative damage in three mutants of Caenorhabditis elegans (age-1, mev-1 and daf-16) that affect life span. Mech Ageing Dev. 2002 Nov;123(12):1579-87. We found that daily short-term exposure (3 h) to hyperoxia further extended the life span of age-1, a phenomenon known as an adaptive response. age-1 also showed resistance to paraquat and heat. We measured mRNA levels of superoxide dismutase genes (sod-1 through 4), catalase genes (clt-1 and ctl-2), known to encode anti-oxidant enzymes, and found they were elevated in age-1 young adults. |
2(0,0,0,2) | Details |
| 19770032 | Peng C, Chan HY, Li YM, Huang Y, Chen ZY: Black tea theaflavins extend the lifespan of fruit flies. Exp Gerontol. 2009 Dec;44(12):773-83. Epub 2009 Sep 19. Gene expression of superoxide dismutase (SOD1 and SOD2), catalase (CAT), and methuselah (MTH) was characterized by an increase in young and then a decrease in aged fruit flies. Paraquat and H (2) O (2) challenge tests demonstrated that BTE prolonged the survival time only for Oregon-R wild type flies but not for SOD (n108) or Cat (n1) mutants. |
2(0,0,0,2) | Details |
| 10036768 | Yoo HY, Kim SS, Rho HM: Overexpression and simple purification of human superoxide dismutase (SOD1) in yeast and its resistance to oxidative stress. J Biotechnol. 1999 Feb 5;68(1):29-35. The yeast overexpressing hSOD1 appeared to be more resistant to oxidative stresses such as paraquat, and heat shock. |
1(0,0,0,1) | Details |
| 16738222 | Santos GM, Afonso V, Barra GB, Togashi M, Webb P, Neves FA, Lomri N, Lomri A: Negative regulation of superoxide dismutase-1 promoter by thyroid hormone. Mol Pharmacol. 2006 Sep;70(3):793-800. Epub 2006 May 31. It is also emerging that T3 is associated with oxidative stress through the regulation of the activity of superoxide dismutase-1 (SOD-1), a key enzyme in the metabolism of free radicals. We found that T3 reverses the activation of the SOD-1 promoter caused by the free radical generators paraquat and phorbol 12- 13- through the direct repression of the SOD-1 promoter by liganded TR. |
1(0,0,0,1) | Details |