Cu Zn superoxide dismutase

Summary

Gene Symbol: Cu Zn superoxide dismutase
Description: superoxide dismutase 1
Alias: ALS, ALS1, HEL-S-44, IPOA, SOD, hSod1, homodimer, superoxide dismutase [Cu-Zn], Cu/Zn superoxide dismutase, SOD, soluble, epididymis secretory protein Li 44, indophenoloxidase A, superoxide dismutase 1, soluble, superoxide dismutase, cystolic
Species: human
Products:     Cu Zn superoxide dismutase

Top Publications

  1. Guo Y, Duan W, Li Z, Huang J, Yin Y, Zhang K, et al. Decreased GLT-1 and increased SOD1 and HO-1 expression in astrocytes contribute to lumbar spinal cord vulnerability of SOD1-G93A transgenic mice. FEBS Lett. 2010;584:1615-22 pubmed publisher
    The SOD1-G93A transgenic mouse is a widely used ALS model, but the death of lower motor neurons is the hallmark...
  2. Nakamura A, Hineno A, Yoshida K, Sekijima Y, Hanaoka Tachibana N, Takei Y, et al. Marked intrafamilial phenotypic variation in a family with SOD1 C111Y mutation. Amyotroph Lateral Scler. 2012;13:479-86 pubmed publisher
    ..Elucidating the biological basis of disease expression in patients with the SOD1 C111Y mutation may provide us with useful information to develop therapeutic approaches and to prevent disease progression. ..
  3. Guareschi S, Cova E, Cereda C, Ceroni M, Donetti E, Bosco D, et al. An over-oxidized form of superoxide dismutase found in sporadic amyotrophic lateral sclerosis with bulbar onset shares a toxic mechanism with mutant SOD1. Proc Natl Acad Sci U S A. 2012;109:5074-9 pubmed publisher
    ..Cu/Zn superoxide dismutase (SOD1) could be pathogenic in both familial and sporadic amyotrophic lateral sclerosis (ALS) through either inheritable or nonheritable modifications...
  4. Forsberg K, Andersen P, Marklund S, Brannstrom T. Glial nuclear aggregates of superoxide dismutase-1 are regularly present in patients with amyotrophic lateral sclerosis. Acta Neuropathol. 2011;121:623-34 pubmed publisher
    The most common cause of amyotrophic lateral sclerosis (ALS) is mutations in superoxide dismutase-1 (SOD1)...
  5. Banci L, Bertini I, Cantini F, Kozyreva T, Massagni C, Palumaa P, et al. Human superoxide dismutase 1 (hSOD1) maturation through interaction with human copper chaperone for SOD1 (hCCS). Proc Natl Acad Sci U S A. 2012;109:13555-60 pubmed publisher
    ..an in vitro model for human CCS-dependent SOD1 maturation based on the study of the interactions of human SOD1 (hSOD1) with full-length WT human CCS (hCCS), as well as with hCCS mutants and various truncated constructs comprising ..
  6. Teilum K, Smith M, Schulz E, Christensen L, Solomentsev G, Oliveberg M, et al. Transient structural distortion of metal-free Cu/Zn superoxide dismutase triggers aberrant oligomerization. Proc Natl Acad Sci U S A. 2009;106:18273-8 pubmed publisher
    Amyotrophic lateral sclerosis (ALS) is a neurodegenerative disease linked to the misfolding of Cu/Zn superoxide dismutase (SOD1). ALS-related defects in SOD1 result in a gain of toxic function that coincides with aberrant oligomerization...
  7. Forsberg K, Jonsson P, Andersen P, Bergemalm D, Graffmo K, Hultdin M, et al. Novel antibodies reveal inclusions containing non-native SOD1 in sporadic ALS patients. PLoS ONE. 2010;5:e11552 pubmed publisher
    Mutations in CuZn-superoxide dismutase (SOD1) cause amyotrophic lateral sclerosis (ALS) and are found in 6% of ALS patients. Non-native and aggregation-prone forms of mutant SOD1s are thought to trigger the disease...
  8. Vassall K, Stubbs H, Primmer H, Tong M, Sullivan S, Sobering R, et al. Decreased stability and increased formation of soluble aggregates by immature superoxide dismutase do not account for disease severity in ALS. Proc Natl Acad Sci U S A. 2011;108:2210-5 pubmed publisher
    Protein aggregation is a hallmark of many diseases, including amyotrophic lateral sclerosis (ALS), where aggregation of Cu/Zn superoxide dismutase (SOD1) is implicated in causing neurodegeneration...
  9. Kerman A, Liu H, Croul S, Bilbao J, Rogaeva E, Zinman L, et al. Amyotrophic lateral sclerosis is a non-amyloid disease in which extensive misfolding of SOD1 is unique to the familial form. Acta Neuropathol. 2010;119:335-44 pubmed publisher
    Amyotrophic lateral sclerosis (ALS) is a conformational disease in which misfolding and aggregation of proteins such as SOD1 (familial ALS) and TDP-43 (sporadic ALS) are central features...

More Information

Publications73

  1. Banci L, Barbieri L, Bertini I, Cantini F, Luchinat E. In-cell NMR in E. coli to monitor maturation steps of hSOD1. PLoS ONE. 2011;6:e23561 pubmed publisher
    ..However, no intramolecular disulfide bridge formation occurs, nor copper uptake, suggesting the need of a specific chaperone for those purposes. ..
  2. Rocha M, Pousinha P, Correia A, Sebastião A, Ribeiro J. Early changes of neuromuscular transmission in the SOD1(G93A) mice model of ALS start long before motor symptoms onset. PLoS ONE. 2013;8:e73846 pubmed publisher
    ..These early changes in the neuromuscular transmission of SOD1(G93A) mice suggest that the ALS associated events start long before symptoms onset.
  3. Elbasiouny S, Amendola J, Durand J, Heckman C. Evidence from computer simulations for alterations in the membrane biophysical properties and dendritic processing of synaptic inputs in mutant superoxide dismutase-1 motoneurons. J Neurosci. 2010;30:5544-58 pubmed publisher
    A critical step in improving our understanding of the development of amyotrophic lateral sclerosis (ALS) is to identify the factors contributing to the alterations in the excitability of motoneurons and assess their individual ..
  4. Ghosh S, Willard B, Comhair S, Dibello P, Xu W, Shiva S, et al. Disulfide bond as a switch for copper-zinc superoxide dismutase activity in asthma. Antioxid Redox Signal. 2013;18:412-23 pubmed publisher
    Loss of superoxide dismutase (SOD) activity is a defining biochemical feature of asthma. However, mechanisms for the reduced activity are unknown...
  5. Richardson K, Allen S, Mortiboys H, Grierson A, Wharton S, Ince P, et al. The effect of SOD1 mutation on cellular bioenergetic profile and viability in response to oxidative stress and influence of mutation-type. PLoS ONE. 2013;8:e68256 pubmed publisher
    Amyotrophic Lateral Sclerosis (ALS) is a fatal neurodegenerative disorder characterized by the progressive degeneration of motor neurons...
  6. Kayatekin C, Zitzewitz J, Matthews C. Disulfide-reduced ALS variants of Cu, Zn superoxide dismutase exhibit increased populations of unfolded species. J Mol Biol. 2010;398:320-31 pubmed publisher
    ..Mutations at dozens of sites in SOD1 induce amyotrophic lateral sclerosis (ALS), a fatal gain-of-function neurodegenerative disease whose molecular basis is unknown...
  7. Marcuzzo S, Zucca I, Mastropietro A, de Rosbo N, Cavalcante P, Tartari S, et al. Hind limb muscle atrophy precedes cerebral neuronal degeneration in G93A-SOD1 mouse model of amyotrophic lateral sclerosis: a longitudinal MRI study. Exp Neurol. 2011;231:30-7 pubmed publisher
    Amyotrophic lateral sclerosis (ALS) is a progressive, fatal, neurodegenerative disorder caused by the degeneration of motor neurons in the CNS, which results in complete paralysis of skeletal muscles...
  8. Pokrishevsky E, Grad L, Yousefi M, Wang J, Mackenzie I, Cashman N. Aberrant localization of FUS and TDP43 is associated with misfolding of SOD1 in amyotrophic lateral sclerosis. PLoS ONE. 2012;7:e35050 pubmed publisher
    Amyotrophic lateral sclerosis (ALS) is incurable and characterized by progressive paralysis of the muscles of the limbs, speech and swallowing, and respiration due to the progressive degeneration of voluntary motor neurons...
  9. Meissner F, Molawi K, Zychlinsky A. Mutant superoxide dismutase 1-induced IL-1beta accelerates ALS pathogenesis. Proc Natl Acad Sci U S A. 2010;107:13046-50 pubmed publisher
    b>ALS is a fatal motor neuron disease of adult onset. Neuroinflammation contributes to ALS disease progression; however, the inflammatory trigger remains unclear...
  10. Graffmo K, Forsberg K, Bergh J, Birve A, Zetterström P, Andersen P, et al. Expression of wild-type human superoxide dismutase-1 in mice causes amyotrophic lateral sclerosis. Hum Mol Genet. 2013;22:51-60 pubmed publisher
    A common cause of amyotrophic lateral sclerosis (ALS) is mutations in the gene encoding superoxide dismutase-1...
  11. Schmidlin T, Kennedy B, Daggett V. Structural changes to monomeric CuZn superoxide dismutase caused by the familial amyotrophic lateral sclerosis-associated mutation A4V. Biophys J. 2009;97:1709-18 pubmed publisher
    Amyotrophic lateral sclerosis (ALS) is a progressive motor neuron degenerative disease, and the inherited form, familial ALS (fALS), has been linked to over 100 different point mutations scattered throughout the Cu-Zn superoxide ..
  12. Israelson A, Arbel N, Da Cruz S, Ilieva H, Yamanaka K, Shoshan Barmatz V, et al. Misfolded mutant SOD1 directly inhibits VDAC1 conductance in a mouse model of inherited ALS. Neuron. 2010;67:575-87 pubmed publisher
    Mutations in superoxide dismutase (SOD1) cause amyotrophic lateral sclerosis (ALS), a neurodegenerative disease characterized by loss of motor neurons...
  13. Pedrini S, Sau D, Guareschi S, Bogush M, Brown R, Naniche N, et al. ALS-linked mutant SOD1 damages mitochondria by promoting conformational changes in Bcl-2. Hum Mol Genet. 2010;19:2974-86 pubmed publisher
    In mutant superoxide dismutase (SOD1)-linked amyotrophic lateral sclerosis (ALS), accumulation of misfolded mutant SOD1 in spinal cord mitochondria is thought to cause mitochondrial dysfunction...
  14. Tortelli R, Conforti F, Cortese R, D Errico E, Distaso E, Mazzei R, et al. Amyotrophic lateral sclerosis: a new missense mutation in the SOD1 gene. Neurobiol Aging. 2013;34:1709.e3-5 pubmed publisher
    Copper-zinc superoxide dismutase-1 (SOD1) is the second most common mutated gene in amyotrophic lateral sclerosis (ALS). To date more than 150 missense mutations of SOD1 have been reported...
  15. Gottfredsen R, Larsen U, Enghild J, Petersen S. Hydrogen peroxide induce modifications of human extracellular superoxide dismutase that results in enzyme inhibition. Redox Biol. 2013;1:24-31 pubmed publisher
    Superoxide dismutase (EC-SOD) controls the level of superoxide in the extracellular space by catalyzing the dismutation of superoxide into hydrogen peroxide and molecular oxygen...
  16. Magrane J, Sahawneh M, Przedborski S, ESTEVEZ A, Manfredi G. Mitochondrial dynamics and bioenergetic dysfunction is associated with synaptic alterations in mutant SOD1 motor neurons. J Neurosci. 2012;32:229-42 pubmed publisher
    ..Together, these results suggest that impaired mitochondrial dynamics may contribute to the selective degeneration of motor neurons in SOD1-FALS. ..
  17. Papa L, Hahn M, Marsh E, Evans B, Germain D. SOD2 to SOD1 switch in breast cancer. J Biol Chem. 2014;289:5412-6 pubmed publisher
    ..We propose that by analogy to the cadherin switch during epithelial-mesenchymal transition, cancer cells also undergo a SOD switch during transformation.
  18. Brotherton T, Polak M, Kelly C, Birve A, Andersen P, Marklund S, et al. A novel ALS SOD1 C6S mutation with implications for aggregation related toxicity and genetic counseling. Amyotroph Lateral Scler. 2011;12:215-9 pubmed publisher
    In this report we describe an ALS family with a novel missense SOD1 mutation with substitution of serine for cysteine at the sixth amino acid (C6S). This mutation has interesting implications for the role of disulfides in causing disease...
  19. Glasauer A, Sena L, Diebold L, Mazar A, Chandel N. Targeting SOD1 reduces experimental non–small-cell lung cancer. J Clin Invest. 2014;124:117-28 pubmed
  20. Pfister T, Sekhon R, White M, Scott P, Munro S, Johnston M, et al. Familial amyotrophic lateral sclerosis in Alberta, Canada. Amyotroph Lateral Scler Frontotemporal Degener. 2013;14:273-7 pubmed publisher
    Systematic review data demonstrate that 5% of ALS cases are familial (FALS). Causative superoxide dismutase-1 (SOD1) mutations are identified in 10-20% of FALS. Few reports of FALS epidemiology exist in Canada...
  21. Prudencio M, Durazo A, Whitelegge J, Borchelt D. An examination of wild-type SOD1 in modulating the toxicity and aggregation of ALS-associated mutant SOD1. Hum Mol Genet. 2010;19:4774-89 pubmed publisher
    ..we demonstrate that the effects of WT SOD1 on the age at which transgenic mice expressing mutant human SOD1 (hSOD1) develop paralysis are influenced by the nature of the ALS mutation and the expression levels of WT hSOD1...
  22. Okamoto Y, Shirakashi Y, Ihara M, Urushitani M, Oono M, Kawamoto Y, et al. Colocalization of 14-3-3 proteins with SOD1 in Lewy body-like hyaline inclusions in familial amyotrophic lateral sclerosis cases and the animal model. PLoS ONE. 2011;6:e20427 pubmed publisher
    ..inclusions inside the anterior horn cells of spinal cords with sporadic amyotrophic lateral sclerosis (ALS)...
  23. Stevens J, Chia R, Hendriks W, Bros Facer V, van Minnen J, Martin J, et al. Modification of superoxide dismutase 1 (SOD1) properties by a GFP tag--implications for research into amyotrophic lateral sclerosis (ALS). PLoS ONE. 2010;5:e9541 pubmed publisher
    Since the discovery that mutations in the enzyme SOD1 are causative in human amyotrophic lateral sclerosis (ALS), many strategies have been employed to elucidate the toxic properties of this ubiquitously expressed mutant protein, ..
  24. Arciello M, Capo C, Cozzolino M, Ferri A, Nencini M, Carri M, et al. Inactivation of cytochrome c oxidase by mutant SOD1s in mouse motoneuronal NSC-34 cells is independent from copper availability but is because of nitric oxide. J Neurochem. 2010;112:183-92 pubmed publisher
    ..Otherwise, the treatment of neuroblastoma x spinal cord cell line-34 expressing G93A, H46R, or H80R hSOD1 mutants, and showing constitutive expression of iNOS and nNOS, with either a NO scavenger, or NOS inhibitors ..
  25. Kuzma Kozakiewicz M, Berdynski M, Morita M, Takahashi Y, Kawata A, Kaida K, et al. Recurrent K3E mutation in Cu/Zn superoxide dismutase gene associated with amyotrophic lateral sclerosis. Amyotroph Lateral Scler Frontotemporal Degener. 2013;14:608-14 pubmed publisher
    ..dismutase (SOD1) gene mutations are the most frequently reported genetic causes of amyotrophic lateral sclerosis (ALS)...
  26. Karch C, Borchelt D. Aggregation modulating elements in mutant human superoxide dismutase 1. Arch Biochem Biophys. 2010;503:175-82 pubmed publisher
    ..Our data suggest that some type of intermolecular interaction between these elements may occur in promoting mutant SOD1 aggregation. ..
  27. Jonsson P, Graffmo K, Andersen P, Marklund S, Brannstrom T. Superoxide dismutase in amyotrophic lateral sclerosis patients homozygous for the D90A mutation. Neurobiol Dis. 2009;36:421-4 pubmed publisher
    The most common of the amyotrophic lateral sclerosis (ALS)-associated superoxide dismutase-1 (SOD1) mutations, D90A, differs from others in its high structural stability and by the existence of both recessive and dominant inheritance...
  28. Stabuc Silih M, Strazisar M, Hawlina M, Glavac D. Absence of pathogenic mutations in VSX1 and SOD1 genes in patients with keratoconus. Cornea. 2010;29:172-6 pubmed publisher
    ..The absence of pathogenic mutations in our large number of unrelated patients with KC indicates that other genetic factors are involved in the development of this disorder. ..
  29. Byström R, Andersen P, Gröbner G, Oliveberg M. SOD1 mutations targeting surface hydrogen bonds promote amyotrophic lateral sclerosis without reducing apo-state stability. J Biol Chem. 2010;285:19544-52 pubmed publisher
    In good accord with the protein aggregation hypothesis for neurodegenerative diseases, ALS-associated SOD1 mutations are found to reduce structural stability or net repulsive charge...
  30. Toichi K, Yamanaka K, Furukawa Y. Disulfide scrambling describes the oligomer formation of superoxide dismutase (SOD1) proteins in the familial form of amyotrophic lateral sclerosis. J Biol Chem. 2013;288:4970-80 pubmed publisher
    ..Based upon our results, therefore, scrambling of the conserved disulfide bond will be a key event to cause the pathological changes in disease-associated mutant SOD1 proteins...
  31. Weisberg S, Lyakhovetsky R, Werdiger A, Gitler A, Soen Y, Kaganovich D. Compartmentalization of superoxide dismutase 1 (SOD1G93A) aggregates determines their toxicity. Proc Natl Acad Sci U S A. 2012;109:15811-6 pubmed
    ..Preventing the accumulation of SOD1G93A in the JUNQ by enhancing its sequestration in an insoluble inclusion reduces the harmful effects of aggregation on cell viability. ..
  32. Haidet Phillips A, Hester M, Miranda C, Meyer K, Braun L, Frakes A, et al. Astrocytes from familial and sporadic ALS patients are toxic to motor neurons. Nat Biotechnol. 2011;29:824-8 pubmed publisher
    Amyotrophic lateral sclerosis (ALS) is a fatal motor neuron disease, with astrocytes implicated as contributing substantially to motor neuron death in familial (F)ALS...
  33. Dangoumau A, Verschueren A, Hammouche E, Papon M, Blasco H, Cherpi Antar C, et al. Novel SOD1 mutation p.V31A identified with a slowly progressive form of amyotrophic lateral sclerosis. Neurobiol Aging. 2014;35:266.e1-4 pubmed publisher
    ..superoxide dismutase 1 (SOD1) protein is mutated in approximately 15% of familial amyotrophic lateral sclerosis (ALS) and 3% of sporadic ALS...
  34. Zetterström P, Graffmo K, Andersen P, Brannstrom T, Marklund S. Composition of soluble misfolded superoxide dismutase-1 in murine models of amyotrophic lateral sclerosis. Neuromolecular Med. 2013;15:147-58 pubmed publisher
    ..They may be the primary cause of toxicity in superoxide dismutase-1-induced amyotrophic lateral sclerosis. ..
  35. Kitamura A, Inada N, Kubota H, Matsumoto G, Kinjo M, Morimoto R, et al. Dysregulation of the proteasome increases the toxicity of ALS-linked mutant SOD1. Genes Cells. 2014;19:209-24 pubmed publisher
    ..In this study, we examined the biophysical properties of amyotrophic lateral sclerosis (ALS)-linked mutations of Cu/Zn superoxide dismutase 1 (SOD1) expressed in human tissue culture cells...
  36. Brown J, Min J, Staropoli J, Collin E, Bi S, Feng X, et al. SOD1, ANG, TARDBP and FUS mutations in amyotrophic lateral sclerosis: a United States clinical testing lab experience. Amyotroph Lateral Scler. 2012;13:217-22 pubmed publisher
    SOD1, ANG, TARDBP and FUS mutations have been associated with amyotrophic lateral sclerosis (ALS)...
  37. Zetterström P, Graffmo K, Andersen P, Brannstrom T, Marklund S. Proteins that bind to misfolded mutant superoxide dismutase-1 in spinal cords from transgenic amyotrophic lateral sclerosis (ALS) model mice. J Biol Chem. 2011;286:20130-6 pubmed publisher
    Mutant superoxide dismutase-1 (SOD1) has an unidentified toxic property that provokes ALS. Several ALS-linked SOD1 mutations cause long C-terminal truncations, which suggests that common cytotoxic SOD1 conformational species should be ..
  38. Durazo A, Shaw B, Chattopadhyay M, Faull K, Nersissian A, Valentine J, et al. Metal-free superoxide dismutase-1 and three different amyotrophic lateral sclerosis variants share a similar partially unfolded beta-barrel at physiological temperature. J Biol Chem. 2009;284:34382-9 pubmed publisher
    ..e. beta3 and beta4, residues 21-53). Together, these results show that human wild-type apo-SOD1 and variants have a partially unfolded beta-barrel at physiological temperature and unfold non-cooperatively. ..
  39. Bosco D, Morfini G, Karabacak N, Song Y, Gros Louis F, Pasinelli P, et al. Wild-type and mutant SOD1 share an aberrant conformation and a common pathogenic pathway in ALS. Nat Neurosci. 2010;13:1396-403 pubmed publisher
    ..In a subset of human sporadic ALS (SALS) cases, motor neurons in the lumbosacral spinal cord were markedly C4F6 immunoreactive, indicating that an ..
  40. Auclair J, Boggio K, Petsko G, Ringe D, Agar J. Strategies for stabilizing superoxide dismutase (SOD1), the protein destabilized in the most common form of familial amyotrophic lateral sclerosis. Proc Natl Acad Sci U S A. 2010;107:21394-9 pubmed publisher
    Amyotrophic lateral sclerosis (ALS) is a disorder characterized by the death of both upper and lower motor neurons and by 3- to 5-yr median survival postdiagnosis...
  41. Prudencio M, Lelie H, Brown H, Whitelegge J, Valentine J, Borchelt D. A novel variant of human superoxide dismutase 1 harboring amyotrophic lateral sclerosis-associated and experimental mutations in metal-binding residues and free cysteines lacks toxicity in vivo. J Neurochem. 2012;121:475-85 pubmed publisher
    ..In cell culture models, we determine that the combined mutation of C6 and C111 to G and S, respectively, dramatically reduces the aggregation propensity of SODMD and may account for the lack of toxicity for this mutant. ..
  42. Barbosa L, Cerqueira F, Macedo A, Garcia C, Angeli J, Schumacher R, et al. Increased SOD1 association with chromatin, DNA damage, p53 activation, and apoptosis in a cellular model of SOD1-linked ALS. Biochim Biophys Acta. 2010;1802:462-71 pubmed publisher
    ..This toxic activity of mutant SOD1 in the nucleus may play an important role in the complex mechanisms associated with motor neuron death observed in ALS pathogenesis.
  43. Gagliardi S, Cova E, Davin A, Guareschi S, Abel K, Alvisi E, et al. SOD1 mRNA expression in sporadic amyotrophic lateral sclerosis. Neurobiol Dis. 2010;39:198-203 pubmed publisher
    ..1.1) is generally recognized as a pathological cause of 20% of the familial form of Amyotrophic Lateral Sclerosis (ALS)...
  44. Zetterström P, Andersen P, Brannstrom T, Marklund S. Misfolded superoxide dismutase-1 in CSF from amyotrophic lateral sclerosis patients. J Neurochem. 2011;117:91-9 pubmed publisher
    Several of the superoxide dismutase-1 (SOD1) mutations linked to amyotrophic lateral sclerosis (ALS) lead to synthesis of structurally defective molecules, suggesting that any cytotoxic conformational species common for all mutations ..
  45. Proctor E, Ding F, Dokholyan N. Structural and thermodynamic effects of post-translational modifications in mutant and wild type Cu, Zn superoxide dismutase. J Mol Biol. 2011;408:555-67 pubmed publisher
  46. Synofzik M, Ronchi D, Keskin I, Basak A, Wilhelm C, Gobbi C, et al. Mutant superoxide dismutase-1 indistinguishable from wild-type causes ALS. Hum Mol Genet. 2012;21:3568-74 pubmed publisher
    A reason for screening amyotrophic lateral sclerosis (ALS) patients for mutations in the superoxide dismutase-1 (SOD1) gene is the opportunity to find novel mutations with properties that can give information on pathogenesis. A novel c...
  47. Vargas M, Johnson D, Johnson J. Decreased glutathione accelerates neurological deficit and mitochondrial pathology in familial ALS-linked hSOD1(G93A) mice model. Neurobiol Dis. 2011;43:543-51 pubmed publisher
    ..Although GCLM(-/-) mice are viable and fertile, the life span of GCLM(-/-)/hSOD1(G93A) mice decreased in 55% when compared to GCLM(+/+)/hSOD1(G93A) mice...
  48. Papadeas S, Kraig S, O Banion C, Lepore A, Maragakis N. Astrocytes carrying the superoxide dismutase 1 (SOD1G93A) mutation induce wild-type motor neuron degeneration in vivo. Proc Natl Acad Sci U S A. 2011;108:17803-8 pubmed publisher
    ..The SOD1(G93A) astrocyte-induced MN death seemed in part mediated by host microglial activation. These findings show that mSOD1 astrocytes alone can induce WT MN death and associated pathological changes in vivo. ..
  49. Prudencio M, Borchelt D. Superoxide dismutase 1 encoding mutations linked to ALS adopts a spectrum of misfolded states. Mol Neurodegener. 2011;6:77 pubmed publisher
    ..An antibody termed hSOD1, which recognizes aa 24-36, detects an epitope shared by soluble non-natively folded WT and mutant SOD1...
  50. Lu L, Wang S, Zheng L, Li X, Suswam E, Zhang X, et al. Amyotrophic lateral sclerosis-linked mutant SOD1 sequesters Hu antigen R (HuR) and TIA-1-related protein (TIAR): implications for impaired post-transcriptional regulation of vascular endothelial growth factor. J Biol Chem. 2009;284:33989-98 pubmed publisher
    ..mouse leads to progressive and selective degeneration of motor neurons similar to amyotrophic lateral sclerosis (ALS)...
  51. Brotherton T, Li Y, Cooper D, Gearing M, Julien J, Rothstein J, et al. Localization of a toxic form of superoxide dismutase 1 protein to pathologically affected tissues in familial ALS. Proc Natl Acad Sci U S A. 2012;109:5505-10 pubmed publisher
    ..In spinal cords from patients with sporadic ALS, other neurodegenerative diseases, and normal controls, C4F6-immunoreactive inclusions were not detected, but the ..
  52. Vonk W, Wijmenga C, Berger R, van De Sluis B, Klomp L. Cu,Zn superoxide dismutase maturation and activity are regulated by COMMD1. J Biol Chem. 2010;285:28991-9000 pubmed publisher
    ..Our present data indicate that homodimer formation is a regulated final step in SOD1 maturation and implicate the recently characterized copper ..
  53. Millecamps S, Salachas F, Cazeneuve C, Gordon P, Bricka B, Camuzat A, et al. SOD1, ANG, VAPB, TARDBP, and FUS mutations in familial amyotrophic lateral sclerosis: genotype-phenotype correlations. J Med Genet. 2010;47:554-60 pubmed publisher
    Mutations in SOD1, ANG, VAPB, TARDBP and FUS genes have been identified in amyotrophic lateral sclerosis (ALS)...
  54. Crippa V, Sau D, Rusmini P, Boncoraglio A, Onesto E, Bolzoni E, et al. The small heat shock protein B8 (HspB8) promotes autophagic removal of misfolded proteins involved in amyotrophic lateral sclerosis (ALS). Hum Mol Genet. 2010;19:3440-56 pubmed publisher
    Several neurodegenerative diseases, including amyotrophic lateral sclerosis (ALS), are characterized by the presence of misfolded proteins, thought to trigger neurotoxicity...
  55. Ip P, Mulligan V, Chakrabartty A. ALS-causing SOD1 mutations promote production of copper-deficient misfolded species. J Mol Biol. 2011;409:839-52 pubmed publisher
    ..SOD1 is a homodimer in which each subunit binds one copper atom and one zinc atom...
  56. Witan H, Gorlovoy P, Kaya A, Koziollek Drechsler I, Neumann H, Behl C, et al. Wild-type Cu/Zn superoxide dismutase (SOD1) does not facilitate, but impedes the formation of protein aggregates of amyotrophic lateral sclerosis causing mutant SOD1. Neurobiol Dis. 2009;36:331-42 pubmed publisher
    ..Aggregation of Cu/Zn superoxide dismutase (SOD1) is a hallmark of a subset of familial amyotrophic lateral sclerosis (ALS) cases. The expression of wild-type SOD1 [SOD(hWT)] surprisingly exacerbates the phenotype of mutant SOD1 in vivo...
  57. Pan L, Yoshii Y, Otomo A, Ogawa H, Iwasaki Y, Shang H, et al. Different human copper-zinc superoxide dismutase mutants, SOD1G93A and SOD1H46R, exert distinct harmful effects on gross phenotype in mice. PLoS ONE. 2012;7:e33409 pubmed publisher
    Amyotrophic lateral sclerosis (ALS) is a heterogeneous group of fatal neurodegenerative diseases characterized by a selective loss of motor neurons in the brain and spinal cord...
  58. Wong M, Martin L. Skeletal muscle-restricted expression of human SOD1 causes motor neuron degeneration in transgenic mice. Hum Mol Genet. 2010;19:2284-302 pubmed publisher
    ..The mechanisms of human SOD1 (hSOD1) toxicity to MNs are unknown...
  59. Magrane J, Hervias I, Henning M, Damiano M, Kawamata H, Manfredi G. Mutant SOD1 in neuronal mitochondria causes toxicity and mitochondrial dynamics abnormalities. Hum Mol Genet. 2009;18:4552-64 pubmed publisher
    Amyotrophic lateral sclerosis (ALS) is a fatal neurological disorder characterized by motor neuron degeneration. Mutations in Cu,Zn-superoxide dismutase (SOD1) are responsible for 20% of familial ALS cases via a toxic gain of function...
  60. Kepp K. Computing stability effects of mutations in human superoxide dismutase 1. J Phys Chem B. 2014;118:1799-812 pubmed publisher
    ..Finally, mutations involving glycine were most difficult to model, of relevance to future method improvement. This could be due to structure changes (glycine has a low structural propensity) or water colocalization with glycine. ..
  61. Pickles S, Vande Velde C. Misfolded SOD1 and ALS: zeroing in on mitochondria. Amyotroph Lateral Scler. 2012;13:333-40 pubmed publisher
    Mutations in SOD1, causative for a subset of familial ALS cases, are associated with the formation of non-normal SOD1 conformers...
  62. Grad L, Guest W, Yanai A, Pokrishevsky E, O Neill M, Gibbs E, et al. Intermolecular transmission of superoxide dismutase 1 misfolding in living cells. Proc Natl Acad Sci U S A. 2011;108:16398-403 pubmed publisher
    ..Expression of the enzymatically inactive, natural familial ALS SOD1 mutations G127X and G85R in human mesenchymal and neural cell lines induces misfolding of wild-type natively ..
  63. Zhao W, Beers D, Henkel J, Zhang W, Urushitani M, Julien J, et al. Extracellular mutant SOD1 induces microglial-mediated motoneuron injury. Glia. 2010;58:231-43 pubmed publisher
    ..dismutase-1 (mSOD1) cause the non-cell-autonomous death of motoneurons in inherited amyotrophic lateral sclerosis (ALS). Microgliosis at sites of motoneuron injury is a neuropathological hallmark of ALS...