NameSuperoxide dismutase [Cu-Zn]
Synonyms
  • 1.15.1.1
  • hSod1
  • Superoxide dismutase 1
Gene NameSOD1
OrganismHuman
Amino acid sequence
>lcl|BSEQ0021851|Superoxide dismutase [Cu-Zn]
MATKAVCVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTEGLHGFHVHEFGDNTAGCTS
AGPHFNPLSRKHGGPKDEERHVGDLGNVTADKDGVADVSIEDSVISLSGDHCIIGRTLVV
HEKADDLGKGGNEESTKTGNAGSRLACGVIGIAQ
Number of residues154
Molecular Weight15935.685
Theoretical pI6.07
GO Classification
Functions
  • identical protein binding
  • zinc ion binding
  • chaperone binding
  • superoxide dismutase activity
  • copper ion binding
  • Rac GTPase binding
  • protein homodimerization activity
  • protein phosphatase 2B binding
Processes
  • regulation of T cell differentiation in thymus
  • positive regulation of apoptotic process
  • peripheral nervous system myelin maintenance
  • response to ethanol
  • regulation of blood pressure
  • auditory receptor cell stereocilium organization
  • cellular response to cadmium ion
  • negative regulation of neuron apoptotic process
  • response to antipsychotic drug
  • response to hydrogen peroxide
  • hydrogen peroxide biosynthetic process
  • transmission of nerve impulse
  • response to copper ion
  • myeloid cell homeostasis
  • sensory perception of sound
  • anterograde axon cargo transport
  • platelet activation
  • embryo implantation
  • neurofilament cytoskeleton organization
  • platelet degranulation
  • response to superoxide
  • glutathione metabolic process
  • retina homeostasis
  • superoxide metabolic process
  • regulation of protein kinase activity
  • response to heat
  • cellular iron ion homeostasis
  • locomotory behavior
  • response to carbon monoxide
  • regulation of GTPase activity
  • spermatogenesis
  • positive regulation of superoxide anion generation
  • response to amphetamine
  • superoxide anion generation
  • response to organic substance
  • response to reactive oxygen species
  • response to nutrient levels
  • heart contraction
  • reactive oxygen species metabolic process
  • ovarian follicle development
  • blood coagulation
  • cellular response to ATP
  • placenta development
  • cellular response to potassium ion
  • regulation of multicellular organism growth
  • cell aging
  • muscle cell cellular homeostasis
  • regulation of organ growth
  • positive regulation of catalytic activity
  • response to drug
  • response to axon injury
  • retrograde axon cargo transport
  • thymus development
  • response to antibiotic
  • regulation of mitochondrial membrane potential
  • negative regulation of cholesterol biosynthetic process
  • positive regulation of oxidative stress-induced intrinsic apoptotic signaling pathway
  • activation of MAPK activity
  • positive regulation of cytokine production
  • removal of superoxide radicals
  • relaxation of vascular smooth muscle
Components
  • extracellular space
  • lysosome
  • cytoplasm
  • cytoplasmic vesicle
  • mitochondrion
  • mitochondrial intermembrane space
  • protein complex
  • dense core granule
  • peroxisome
  • extracellular matrix
  • dendrite cytoplasm
  • extracellular region
  • cytosol
  • nucleus
  • neuronal cell body
  • extracellular exosome
  • myelin sheath
  • mitochondrial matrix
  • nucleoplasm
General FunctionZinc ion binding
Specific FunctionDestroys radicals which are normally produced within the cells and which are toxic to biological systems.
Pfam Domain Function
Transmembrane RegionsNot Available
GenBank Protein IDNot Available
UniProtKB IDP00441
UniProtKB Entry NameSODC_HUMAN
Cellular LocationCytoplasm
Gene sequence
>lcl|BSEQ0021852|Superoxide dismutase [Cu-Zn] (SOD1)
ATGGCGACGAAGGCCGTGTGCGTGCTGAAGGGCGACGGCCCAGTGCAGGGCATCATCAAT
TTCGAGCAGAAGGAAAGTAATGGACCAGTGAAGGTGTGGGGAAGCATTAAAGGACTGACT
GAAGGCCTGCATGGATTCCATGTTCATGAGTTTGGAGATAATACAGCAGGCTGTACCAGT
GCAGGTCCTCACTTTAATCCTCTATCCAGAAAACACGGTGGGCCAAAGGATGAAGAGAGG
CATGTTGGAGACTTGGGCAATGTGACTGCTGACAAAGATGGTGTGGCCGATGTGTCTATT
GAAGATTCTGTGATCTCACTCTCAGGAGACCATTGCATCATTGGCCGCACACTGGTGGTC
CATGAAAAAGCAGATGACTTGGGCAAAGGTGGAAATGAAGAAAGTACAAAGACAGGAAAC
GCTGGAAGTCGTTTGGCTTGTGGTGTAATTGGGATCGCCCAATAA
GenBank Gene IDL44139
GeneCard IDNot Available
GenAtlas IDSOD1
HGNC IDHGNC:11179
Chromosome Location21
LocusNot Available
References
  1. Sherman L, Dafni N, Lieman-Hurwitz J, Groner Y: Nucleotide sequence and expression of human chromosome 21-encoded superoxide dismutase mRNA. Proc Natl Acad Sci U S A. 1983 Sep;80(18):5465-9. 6577438
  2. Levanon D, Lieman-Hurwitz J, Dafni N, Wigderson M, Sherman L, Bernstein Y, Laver-Rudich Z, Danciger E, Stein O, Groner Y: Architecture and anatomy of the chromosomal locus in human chromosome 21 encoding the Cu/Zn superoxide dismutase. EMBO J. 1985 Jan;4(1):77-84. 3160582
  3. Hallewell RA, Masiarz FR, Najarian RC, Puma JP, Quiroga MR, Randolph A, Sanchez-Pescador R, Scandella CJ, Smith B, Steimer KS, et al.: Human Cu/Zn superoxide dismutase cDNA: isolation of clones synthesising high levels of active or inactive enzyme from an expression library. Nucleic Acids Res. 1985 Mar 25;13(6):2017-34. 3889846
  4. Kajihara J, Enomoto M, Nishijima K, Yabuuchi M, Katoh K: Comparison of properties between human recombinant and placental copper-zinc SOD. J Biochem. 1988 Nov;104(5):851-4. 2853161
  5. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. 14702039
  6. Hattori M, Fujiyama A, Taylor TD, Watanabe H, Yada T, Park HS, Toyoda A, Ishii K, Totoki Y, Choi DK, Groner Y, Soeda E, Ohki M, Takagi T, Sakaki Y, Taudien S, Blechschmidt K, Polley A, Menzel U, Delabar J, Kumpf K, Lehmann R, Patterson D, Reichwald K, Rump A, Schillhabel M, Schudy A, Zimmermann W, Rosenthal A, Kudoh J, Schibuya K, Kawasaki K, Asakawa S, Shintani A, Sasaki T, Nagamine K, Mitsuyama S, Antonarakis SE, Minoshima S, Shimizu N, Nordsiek G, Hornischer K, Brant P, Scharfe M, Schon O, Desario A, Reichelt J, Kauer G, Blocker H, Ramser J, Beck A, Klages S, Hennig S, Riesselmann L, Dagand E, Haaf T, Wehrmeyer S, Borzym K, Gardiner K, Nizetic D, Francis F, Lehrach H, Reinhardt R, Yaspo ML: The DNA sequence of human chromosome 21. Nature. 2000 May 18;405(6784):311-9. 10830953
  7. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. 15489334
  8. Jabusch JR, Farb DL, Kerschensteiner DA, Deutsch HF: Some sulfhydryl properties and primary structure of human erythrocyte superoxide dismutase. Biochemistry. 1980 May 27;19(11):2310-6. 6770891
  9. Barra D, Martini F, Bannister JV, Schinina ME, Rotilio G, Bannister WH, Bossa F: The complete amino acid sequence of human Cu/Zn superoxide dismutase. FEBS Lett. 1980 Oct 20;120(1):53-6. 7002610
  10. Enayat ZE, Orrell RW, Claus A, Ludolph A, Bachus R, Brockmuller J, Ray-Chaudhuri K, Radunovic A, Shaw C, Wilkinson J, et al.: Two novel mutations in the gene for copper zinc superoxide dismutase in UK families with amyotrophic lateral sclerosis. Hum Mol Genet. 1995 Jul;4(7):1239-40. 8528216
  11. Kostrzewa M, Damian MS, Muller U: Superoxide dismutase 1: identification of a novel mutation in a case of familial amyotrophic lateral sclerosis. Hum Genet. 1996 Jul;98(1):48-50. 8682505
  12. Arnesano F, Banci L, Bertini I, Martinelli M, Furukawa Y, O'Halloran TV: The unusually stable quaternary structure of human Cu,Zn-superoxide dismutase 1 is controlled by both metal occupancy and disulfide status. J Biol Chem. 2004 Nov 12;279(46):47998-8003. Epub 2004 Aug 23. 15326189
  13. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. doi: 10.1073/pnas.0805139105. Epub 2008 Jul 31. 18669648
  14. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. doi: 10.1126/science.1175371. Epub 2009 Jul 16. 19608861
  15. Medinas DB, Gozzo FC, Santos LF, Iglesias AH, Augusto O: A ditryptophan cross-link is responsible for the covalent dimerization of human superoxide dismutase 1 during its bicarbonate-dependent peroxidase activity. Free Radic Biol Med. 2010 Sep 15;49(6):1046-53. doi: 10.1016/j.freeradbiomed.2010.06.018. Epub 2010 Jun 30. 20600836
  16. Olsen JV, Vermeulen M, Santamaria A, Kumar C, Miller ML, Jensen LJ, Gnad F, Cox J, Jensen TS, Nigg EA, Brunak S, Mann M: Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis. Sci Signal. 2010 Jan 12;3(104):ra3. doi: 10.1126/scisignal.2000475. 20068231
  17. Burkard TR, Planyavsky M, Kaupe I, Breitwieser FP, Burckstummer T, Bennett KL, Superti-Furga G, Colinge J: Initial characterization of the human central proteome. BMC Syst Biol. 2011 Jan 26;5:17. doi: 10.1186/1752-0509-5-17. 21269460
  18. Marin EP, Derakhshan B, Lam TT, Davalos A, Sessa WC: Endothelial cell palmitoylproteomic identifies novel lipid-modified targets and potential substrates for protein acyl transferases. Circ Res. 2012 May 11;110(10):1336-44. doi: 10.1161/CIRCRESAHA.112.269514. Epub 2012 Apr 10. 22496122
  19. Rosenow A, Noben JP, Jocken J, Kallendrusch S, Fischer-Posovszky P, Mariman EC, Renes J: Resveratrol-induced changes of the human adipocyte secretion profile. J Proteome Res. 2012 Sep 7;11(9):4733-43. doi: 10.1021/pr300539b. Epub 2012 Aug 27. 22905912
  20. Lin ZF, Xu HB, Wang JY, Lin Q, Ruan Z, Liu FB, Jin W, Huang HH, Chen X: SIRT5 desuccinylates and activates SOD1 to eliminate ROS. Biochem Biophys Res Commun. 2013 Nov 8;441(1):191-5. doi: 10.1016/j.bbrc.2013.10.033. Epub 2013 Oct 16. 24140062
  21. Banci L, Cantini F, Kozyreva T, Rubino JT: Mechanistic aspects of hSOD1 maturation from the solution structure of Cu(I) -loaded hCCS domain 1 and analysis of disulfide-free hSOD1 mutants. Chembiochem. 2013 Sep 23;14(14):1839-44. doi: 10.1002/cbic.201300042. Epub 2013 Apr 26. 23625804
  22. Bian Y, Song C, Cheng K, Dong M, Wang F, Huang J, Sun D, Wang L, Ye M, Zou H: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome. J Proteomics. 2014 Jan 16;96:253-62. doi: 10.1016/j.jprot.2013.11.014. Epub 2013 Nov 22. 24275569
  23. Vaca Jacome AS, Rabilloud T, Schaeffer-Reiss C, Rompais M, Ayoub D, Lane L, Bairoch A, Van Dorsselaer A, Carapito C: N-terminome analysis of the human mitochondrial proteome. Proteomics. 2015 Jul;15(14):2519-24. doi: 10.1002/pmic.201400617. Epub 2015 Jun 8. 25944712
  24. Parge HE, Hallewell RA, Tainer JA: Atomic structures of wild-type and thermostable mutant recombinant human Cu,Zn superoxide dismutase. Proc Natl Acad Sci U S A. 1992 Jul 1;89(13):6109-13. 1463506
  25. Hart PJ, Liu H, Pellegrini M, Nersissian AM, Gralla EB, Valentine JS, Eisenberg D: Subunit asymmetry in the three-dimensional structure of a human CuZnSOD mutant found in familial amyotrophic lateral sclerosis. Protein Sci. 1998 Mar;7(3):545-55. 9541385
  26. Banci L, Benedetto M, Bertini I, Del Conte R, Piccioli M, Viezzoli MS: Solution structure of reduced monomeric Q133M2 copper, zinc superoxide dismutase (SOD). Why is SOD a dimeric enzyme?. Biochemistry. 1998 Aug 25;37(34):11780-91. 9718300
  27. Ferraroni M, Rypniewski W, Wilson KS, Viezzoli MS, Banci L, Bertini I, Mangani S: The crystal structure of the monomeric human SOD mutant F50E/G51E/E133Q at atomic resolution. The enzyme mechanism revisited. J Mol Biol. 1999 May 7;288(3):413-26. 10329151
  28. Banci L, Bertini I, Cramaro F, Del Conte R, Viezzoli MS: Solution structure of Apo Cu,Zn superoxide dismutase: role of metal ions in protein folding. Biochemistry. 2003 Aug 19;42(32):9543-53. 12911296
  29. DiDonato M, Craig L, Huff ME, Thayer MM, Cardoso RM, Kassmann CJ, Lo TP, Bruns CK, Powers ET, Kelly JW, Getzoff ED, Tainer JA: ALS mutants of human superoxide dismutase form fibrous aggregates via framework destabilization. J Mol Biol. 2003 Sep 19;332(3):601-15. 12963370
  30. Elam JS, Taylor AB, Strange R, Antonyuk S, Doucette PA, Rodriguez JA, Hasnain SS, Hayward LJ, Valentine JS, Yeates TO, Hart PJ: Amyloid-like filaments and water-filled nanotubes formed by SOD1 mutant proteins linked to familial ALS. Nat Struct Biol. 2003 Jun;10(6):461-7. 12754496
  31. Hough MA, Grossmann JG, Antonyuk SV, Strange RW, Doucette PA, Rodriguez JA, Whitson LJ, Hart PJ, Hayward LJ, Valentine JS, Hasnain SS: Dimer destabilization in superoxide dismutase may result in disease-causing properties: structures of motor neuron disease mutants. Proc Natl Acad Sci U S A. 2004 Apr 20;101(16):5976-81. Epub 2004 Mar 31. 15056757
  32. Banci L, Bertini I, Cantini F, D'Amelio N, Gaggelli E: Human SOD1 before harboring the catalytic metal: solution structure of copper-depleted, disulfide-reduced form. J Biol Chem. 2006 Jan 27;281(4):2333-7. Epub 2005 Nov 14. 16291742
  33. Strange RW, Antonyuk SV, Hough MA, Doucette PA, Valentine JS, Hasnain SS: Variable metallation of human superoxide dismutase: atomic resolution crystal structures of Cu-Zn, Zn-Zn and as-isolated wild-type enzymes. J Mol Biol. 2006 Mar 10;356(5):1152-62. Epub 2005 Dec 12. 16406071
  34. Hornberg A, Logan DT, Marklund SL, Oliveberg M: The coupling between disulphide status, metallation and dimer interface strength in Cu/Zn superoxide dismutase. J Mol Biol. 2007 Jan 12;365(2):333-42. Epub 2006 Sep 23. 17070542
  35. Roberts BR, Tainer JA, Getzoff ED, Malencik DA, Anderson SR, Bomben VC, Meyers KR, Karplus PA, Beckman JS: Structural characterization of zinc-deficient human superoxide dismutase and implications for ALS. J Mol Biol. 2007 Nov 2;373(4):877-90. Epub 2007 Aug 2. 17888947
  36. Strange RW, Yong CW, Smith W, Hasnain SS: Molecular dynamics using atomic-resolution structure reveal structural fluctuations that may lead to polymerization of human Cu-Zn superoxide dismutase. Proc Natl Acad Sci U S A. 2007 Jun 12;104(24):10040-4. Epub 2007 Jun 4. 17548825
  37. Cao X, Antonyuk SV, Seetharaman SV, Whitson LJ, Taylor AB, Holloway SP, Strange RW, Doucette PA, Valentine JS, Tiwari A, Hayward LJ, Padua S, Cohlberg JA, Hasnain SS, Hart PJ: Structures of the G85R variant of SOD1 in familial amyotrophic lateral sclerosis. J Biol Chem. 2008 Jun 6;283(23):16169-77. doi: 10.1074/jbc.M801522200. Epub 2008 Mar 31. 18378676
  38. de Belleroche J, Orrell R, King A: Familial amyotrophic lateral sclerosis/motor neurone disease (FALS): a review of current developments. J Med Genet. 1995 Nov;32(11):841-7. 8592323
  39. Seetharaman SV, Taylor AB, Holloway S, Hart PJ: Structures of mouse SOD1 and human/mouse SOD1 chimeras. Arch Biochem Biophys. 2010 Nov 15;503(2):183-90. doi: 10.1016/j.abb.2010.08.014. Epub 2010 Aug 19. 20727846
  40. Rosen DR, Siddique T, Patterson D, Figlewicz DA, Sapp P, Hentati A, Donaldson D, Goto J, O'Regan JP, Deng HX, et al.: Mutations in Cu/Zn superoxide dismutase gene are associated with familial amyotrophic lateral sclerosis. Nature. 1993 Mar 4;362(6415):59-62. 8446170
  41. Rosen DR: Mutations in Cu/Zn superoxide dismutase gene are associated with familial amyotrophic lateral sclerosis. Nature. 1993 Jul 22;364(6435):362. 8332197
  42. Deng HX, Hentati A, Tainer JA, Iqbal Z, Cayabyab A, Hung WY, Getzoff ED, Hu P, Herzfeldt B, Roos RP, et al.: Amyotrophic lateral sclerosis and structural defects in Cu,Zn superoxide dismutase. Science. 1993 Aug 20;261(5124):1047-51. 8351519
  43. Nakano R, Sato S, Inuzuka T, Sakimura K, Mishina M, Takahashi H, Ikuta F, Honma Y, Fujii J, Taniguchi N, et al.: A novel mutation in Cu/Zn superoxide dismutase gene in Japanese familial amyotrophic lateral sclerosis. Biochem Biophys Res Commun. 1994 Apr 29;200(2):695-703. 8179602
  44. Hirano M, Fujii J, Nagai Y, Sonobe M, Okamoto K, Araki H, Taniguchi N, Ueno S: A new variant Cu/Zn superoxide dismutase (Val7-->Glu) deduced from lymphocyte mRNA sequences from Japanese patients with familial amyotrophic lateral sclerosis. Biochem Biophys Res Commun. 1994 Oct 28;204(2):572-7. 7980516
  45. Jones CT, Swingler RJ, Brock DJ: Identification of a novel SOD1 mutation in an apparently sporadic amyotrophic lateral sclerosis patient and the detection of Ile113Thr in three others. Hum Mol Genet. 1994 Apr;3(4):649-50. 8069312
  46. Esteban J, Rosen DR, Bowling AC, Sapp P, McKenna-Yasek D, O'Regan JP, Beal MF, Horvitz HR, Brown RH Jr: Identification of two novel mutations and a new polymorphism in the gene for Cu/Zn superoxide dismutase in patients with amyotrophic lateral sclerosis. Hum Mol Genet. 1994 Jun;3(6):997-8. 7951252
  47. Kostrzewa M, Burck-Lehmann U, Muller U: Autosomal dominant amyotrophic lateral sclerosis: a novel mutation in the Cu/Zn superoxide dismutase-1 gene. Hum Mol Genet. 1994 Dec;3(12):2261-2. 7881433
  48. Aoki M, Ogasawara M, Matsubara Y, Narisawa K, Nakamura S, Itoyama Y, Abe K: Familial amyotrophic lateral sclerosis (ALS) in Japan associated with H46R mutation in Cu/Zn superoxide dismutase gene: a possible new subtype of familial ALS. J Neurol Sci. 1994 Oct;126(1):77-83. 7836951
  49. Suthers G, Laing N, Wilton S, Dorosz S, Waddy H: "Sporadic" motoneuron disease due to familial SOD1 mutation with low penetrance. Lancet. 1994 Dec 24-31;344(8939-8940):1773. 7997024
  50. Jones CT, Shaw PJ, Chari G, Brock DJ: Identification of a novel exon 4 SOD1 mutation in a sporadic amyotrophic lateral sclerosis patient. Mol Cell Probes. 1994 Aug;8(4):329-30. 7870076
  51. Pramatarova A, Figlewicz DA, Krizus A, Han FY, Ceballos-Picot I, Nicole A, Dib M, Meininger V, Brown RH, Rouleau GA: Identification of new mutations in the Cu/Zn superoxide dismutase gene of patients with familial amyotrophic lateral sclerosis. Am J Hum Genet. 1995 Mar;56(3):592-6. 7887412
  52. Ikeda M, Abe K, Aoki M, Ogasawara M, Kameya T, Watanabe M, Shoji M, Hirai S, Itoyama Y: A novel point mutation in the Cu/Zn superoxide dismutase gene in a patient with familial amyotrophic lateral sclerosis. Hum Mol Genet. 1995 Mar;4(3):491-2. 7795609
  53. Yulug IG, Katsanis N, de Belleroche J, Collinge J, Fisher EM: An improved protocol for the analysis of SOD1 gene mutations, and a new mutation in exon 4. Hum Mol Genet. 1995 Jun;4(6):1101-4. 7655468
  54. Sjalander A, Beckman G, Deng HX, Iqbal Z, Tainer JA, Siddique T: The D90A mutation results in a polymorphism of Cu,Zn superoxide dismutase that is prevalent in northern Sweden and Finland. Hum Mol Genet. 1995 Jun;4(6):1105-8. 7655469
  55. Deng HX, Tainer JA, Mitsumoto H, Ohnishi A, He X, Hung WY, Zhao Y, Juneja T, Hentati A, Siddique T: Two novel SOD1 mutations in patients with familial amyotrophic lateral sclerosis. Hum Mol Genet. 1995 Jun;4(6):1113-6. 7655471
  56. Orrell R, de Belleroche J, Marklund S, Bowe F, Hallewell R: A novel SOD mutant and ALS. Nature. 1995 Apr 6;374(6522):504-5. 7700376
  57. Andersen PM, Nilsson P, Ala-Hurula V, Keranen ML, Tarvainen I, Haltia T, Nilsson L, Binzer M, Forsgren L, Marklund SL: Amyotrophic lateral sclerosis associated with homozygosity for an Asp90Ala mutation in CuZn-superoxide dismutase. Nat Genet. 1995 May;10(1):61-6. 7647793
  58. Ikeda M, Abe K, Aoki M, Sahara M, Watanabe M, Shoji M, St George-Hyslop PH, Hirai S, Itoyama Y: Variable clinical symptoms in familial amyotrophic lateral sclerosis with a novel point mutation in the Cu/Zn superoxide dismutase gene. Neurology. 1995 Nov;45(11):2038-42. 7501156
  59. Sapp PC, Rosen DR, Hosler BA, Esteban J, McKenna-Yasek D, O'Regan JP, Horvitz HR, Brown RH Jr: Identification of three novel mutations in the gene for Cu/Zn superoxide dismutase in patients with familial amyotrophic lateral sclerosis. Neuromuscul Disord. 1995 Sep;5(5):353-7. 7496169
  60. Hosler BA, Nicholson GA, Sapp PC, Chin W, Orrell RW, de Belleroche JS, Esteban J, Hayward LJ, Mckenna-Yasek D, Yeung L, Cherryson AK, Dench JE, Wilton SD, Laing NG, Horvitz HR, Brown RH Jr: Three novel mutations and two variants in the gene for Cu/Zn superoxide dismutase in familial amyotrophic lateral sclerosis. Neuromuscul Disord. 1996 Oct;6(5):361-6. 8938700
  61. Morita M, Aoki M, Abe K, Hasegawa T, Sakuma R, Onodera Y, Ichikawa N, Nishizawa M, Itoyama Y: A novel two-base mutation in the Cu/Zn superoxide dismutase gene associated with familial amyotrophic lateral sclerosis in Japan. Neurosci Lett. 1996 Feb 23;205(2):79-82. 8907321
  62. Watanabe M, Aoki M, Abe K, Shoji M, Iizuka T, Ikeda Y, Hirai S, Kurokawa K, Kato T, Sasaki H, Itoyama Y: A novel missense point mutation (S134N) of the Cu/Zn superoxide dismutase gene in a patient with familial motor neuron disease. Hum Mutat. 1997;9(1):69-71. 8990014
  63. Kawamata J, Shimohama S, Takano S, Harada K, Ueda K, Kimura J: Novel G16S (GGC-AGC) mutation in the SOD-1 gene in a patient with apparently sporadic young-onset amyotrophic lateral sclerosis. Hum Mutat. 1997;9(4):356-8. 9101297
  64. Orrell RW, Marklund SL, deBelleroche JS: Familial ALS is associated with mutations in all exons of SOD1: a novel mutation in exon 3 (Gly72Ser). J Neurol Sci. 1997 Dec 9;153(1):46-9. 9455977
  65. Kikugawa K, Nakano R, Inuzuka T, Kokubo Y, Narita Y, Kuzuhara S, Yoshida S, Tsuji S: A missense mutation in the SOD1 gene in patients with amyotrophic lateral sclerosis from the Kii Peninsula and its vicinity, Japan. Neurogenetics. 1997 Sep;1(2):113-5. 10732812
  66. Bereznai B, Winkler A, Borasio GD, Gasser T: A novel SOD1 mutation in an Austrian family with amyotrophic lateral sclerosis. Neuromuscul Disord. 1997 Mar;7(2):113-6. 9131652
  67. Ratovitski T, Corson LB, Strain J, Wong P, Cleveland DW, Culotta VC, Borchelt DR: Variation in the biochemical/biophysical properties of mutant superoxide dismutase 1 enzymes and the rate of disease progression in familial amyotrophic lateral sclerosis kindreds. Hum Mol Genet. 1999 Aug;8(8):1451-60. 10400992
  68. Penco S, Schenone A, Bordo D, Bolognesi M, Abbruzzese M, Bugiani O, Ajmar F, Garre C: A SOD1 gene mutation in a patient with slowly progressing familial ALS. Neurology. 1999 Jul 22;53(2):404-6. 10430435
  69. Murakami T, Warita H, Hayashi T, Sato K, Manabe Y, Mizuno S, Yamane K, Abe K: A novel SOD1 gene mutation in familial ALS with low penetrance in females. J Neurol Sci. 2001 Aug 15;189(1-2):45-7. 11535232
  70. Gellera C, Castellotti B, Riggio MC, Silani V, Morandi L, Testa D, Casali C, Taroni F, Di Donato S, Zeviani M, Mariotti C: Superoxide dismutase gene mutations in Italian patients with familial and sporadic amyotrophic lateral sclerosis: identification of three novel missense mutations. Neuromuscul Disord. 2001 May;11(4):404-10. 11369193
  71. Alexander MD, Traynor BJ, Miller N, Corr B, Frost E, McQuaid S, Brett FM, Green A, Hardiman O: "True" sporadic ALS associated with a novel SOD-1 mutation. Ann Neurol. 2002 Nov;52(5):680-3. 12402272
  72. Niwa J, Ishigaki S, Hishikawa N, Yamamoto M, Doyu M, Murata S, Tanaka K, Taniguchi N, Sobue G: Dorfin ubiquitylates mutant SOD1 and prevents mutant SOD1-mediated neurotoxicity. J Biol Chem. 2002 Sep 27;277(39):36793-8. Epub 2002 Jul 26. 12145308
  73. Andersen PM, Sims KB, Xin WW, Kiely R, O'Neill G, Ravits J, Pioro E, Harati Y, Brower RD, Levine JS, Heinicke HU, Seltzer W, Boss M, Brown RH Jr: Sixteen novel mutations in the Cu/Zn superoxide dismutase gene in amyotrophic lateral sclerosis: a decade of discoveries, defects and disputes. Amyotroph Lateral Scler Other Motor Neuron Disord. 2003 Jun;4(2):62-73. 14506936
  74. Furukawa Y, Kaneko K, Yamanaka K, O'Halloran TV, Nukina N: Complete loss of post-translational modifications triggers fibrillar aggregation of SOD1 in the familial form of amyotrophic lateral sclerosis. J Biol Chem. 2008 Aug 29;283(35):24167-76. doi: 10.1074/jbc.M802083200. Epub 2008 Jun 13. 18552350
  75. Banci L, Bertini I, Boca M, Girotto S, Martinelli M, Valentine JS, Vieru M: SOD1 and amyotrophic lateral sclerosis: mutations and oligomerization. PLoS One. 2008 Feb 27;3(2):e1677. doi: 10.1371/journal.pone.0001677. 18301754
  76. Yonashiro R, Sugiura A, Miyachi M, Fukuda T, Matsushita N, Inatome R, Ogata Y, Suzuki T, Dohmae N, Yanagi S: Mitochondrial ubiquitin ligase MITOL ubiquitinates mutant SOD1 and attenuates mutant SOD1-induced reactive oxygen species generation. Mol Biol Cell. 2009 Nov;20(21):4524-30. doi: 10.1091/mbc.E09-02-0112. Epub 2009 Sep 9. 19741096
  77. del Grande A, Luigetti M, Conte A, Mancuso I, Lattante S, Marangi G, Stipa G, Zollino M, Sabatelli M: A novel L67P SOD1 mutation in an Italian ALS patient. Amyotroph Lateral Scler. 2011 Mar;12(2):150-2. doi: 10.3109/17482968.2011.551939. Epub 2011 Jan 19. 21247266
  78. Chio A, Borghero G, Pugliatti M, Ticca A, Calvo A, Moglia C, Mutani R, Brunetti M, Ossola I, Marrosu MG, Murru MR, Floris G, Cannas A, Parish LD, Cossu P, Abramzon Y, Johnson JO, Nalls MA, Arepalli S, Chong S, Hernandez DG, Traynor BJ, Restagno G: Large proportion of amyotrophic lateral sclerosis cases in Sardinia due to a single founder mutation of the TARDBP gene. Arch Neurol. 2011 May;68(5):594-8. doi: 10.1001/archneurol.2010.352. Epub 2011 Jan 10. 21220647