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'''Unreleased structure'''


The entry 3ecv is ON HOLD  until Paper Publication
==Crystal structure of the ALS-related pathological mutant I113T of human apo Cu,Zn Superoxide Dismutase (SOD1)==
<StructureSection load='3ecv' size='340' side='right'caption='[[3ecv]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3ecv]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ECV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ECV FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3ecv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ecv OCA], [https://pdbe.org/3ecv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ecv RCSB], [https://www.ebi.ac.uk/pdbsum/3ecv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ecv ProSAT]</span></td></tr>
</table>
== Disease ==
[https://www.uniprot.org/uniprot/SODC_HUMAN SODC_HUMAN] Defects in SOD1 are the cause of amyotrophic lateral sclerosis type 1 (ALS1) [MIM:[https://omim.org/entry/105400 105400]. ALS1 is a familial form of amyotrophic lateral sclerosis, a neurodegenerative disorder affecting upper and lower motor neurons and resulting in fatal paralysis. Sensory abnormalities are absent. Death usually occurs within 2 to 5 years. The etiology of amyotrophic lateral sclerosis is likely to be multifactorial, involving both genetic and environmental factors. The disease is inherited in 5-10% of cases leading to familial forms.<ref>PMID:12963370</ref> <ref>PMID:19741096</ref> <ref>PMID:8528216</ref> <ref>PMID:8682505</ref> <ref>PMID:9541385</ref> <ref>PMID:12754496</ref> <ref>PMID:15056757</ref> <ref>PMID:18378676</ref> [:]<ref>PMID:8446170</ref> <ref>PMID:8351519</ref> <ref>PMID:8179602</ref> <ref>PMID:7980516</ref> <ref>PMID:8069312</ref> <ref>PMID:7951252</ref> <ref>PMID:7881433</ref> <ref>PMID:7836951</ref> <ref>PMID:7997024</ref> <ref>PMID:7870076</ref> <ref>PMID:7887412</ref> <ref>PMID:7795609</ref> <ref>PMID:7655468</ref> <ref>PMID:7655469</ref> <ref>PMID:7655471</ref> <ref>PMID:7700376</ref> <ref>PMID:7647793</ref> <ref>PMID:7501156</ref> <ref>PMID:7496169</ref> <ref>PMID:8938700</ref> <ref>PMID:8907321</ref> <ref>PMID:8990014</ref> <ref>PMID:9101297</ref> <ref>PMID:9455977</ref> <ref>PMID:10732812</ref> <ref>PMID:9131652</ref> <ref>PMID:10400992</ref> <ref>PMID:10430435</ref> <ref>PMID:11535232</ref> <ref>PMID:11369193</ref> <ref>PMID:12402272</ref> <ref>PMID:12145308</ref> <ref>PMID:14506936</ref> <ref>PMID:18552350</ref> <ref>PMID:18301754</ref> <ref>PMID:21247266</ref> <ref>PMID:21220647</ref>
== Function ==
[https://www.uniprot.org/uniprot/SODC_HUMAN SODC_HUMAN] Destroys radicals which are normally produced within the cells and which are toxic to biological systems.
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ec/3ecv_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3ecv ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The structural and dynamical properties of the metal-free form of WT human superoxide dismutase 1 (SOD1) and its familial amyotrophic lateral sclerosis (fALS)-related mutants, T54R and I113T, were characterized both in solution, through NMR, and in the crystal, through X-ray diffraction. We found that all 3 X-ray structures show significant structural disorder in 2 loop regions that are, at variance, well defined in the fully-metalated structures. Interestingly, the apo state crystallizes only at low temperatures, whereas all 3 proteins in the metalated form crystallize at any temperature, suggesting that crystallization selects one of the most stable conformations among the manifold adopted by the apo form in solution. Indeed, NMR experiments show that the protein in solution is highly disordered, sampling a large range of conformations. The large conformational variability of the apo state allows the free reduced cysteine Cys-6 to become highly solvent accessible in solution, whereas it is essentially buried in the metalated state and the crystal structures. Such solvent accessibility, together with that of Cys-111, accounts for the tendency to oligomerization of the metal-free state. The present results suggest that the investigation of the solution state coupled with that of the crystal state can provide major insights into SOD1 pathway toward oligomerization in relation to fALS.


Authors: Calderone, V.
Structural and dynamic aspects related to oligomerization of apo SOD1 and its mutants.,Banci L, Bertini I, Boca M, Calderone V, Cantini F, Girotto S, Vieru M Proc Natl Acad Sci U S A. 2009 Apr 28;106(17):6980-5. Epub 2009 Apr 14. PMID:19369197<ref>PMID:19369197</ref>


Description: Crystal structure of the ALS-related pathological mutant I113T of human apo Cu,Zn Superoxide Dismutase (SOD1)
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3ecv" style="background-color:#fffaf0;"></div>


''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Nov 20 07:38:52 2008''
==See Also==
*[[Superoxide dismutase 3D structures|Superoxide dismutase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Calderone V]]

Latest revision as of 04:45, 21 November 2024

Crystal structure of the ALS-related pathological mutant I113T of human apo Cu,Zn Superoxide Dismutase (SOD1)Crystal structure of the ALS-related pathological mutant I113T of human apo Cu,Zn Superoxide Dismutase (SOD1)

Structural highlights

3ecv is a 4 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.9Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

SODC_HUMAN Defects in SOD1 are the cause of amyotrophic lateral sclerosis type 1 (ALS1) [MIM:105400. ALS1 is a familial form of amyotrophic lateral sclerosis, a neurodegenerative disorder affecting upper and lower motor neurons and resulting in fatal paralysis. Sensory abnormalities are absent. Death usually occurs within 2 to 5 years. The etiology of amyotrophic lateral sclerosis is likely to be multifactorial, involving both genetic and environmental factors. The disease is inherited in 5-10% of cases leading to familial forms.[1] [2] [3] [4] [5] [6] [7] [8] [:][9] [10] [11] [12] [13] [14] [15] [16] [17] [18] [19] [20] [21] [22] [23] [24] [25] [26] [27] [28] [29] [30] [31] [32] [33] [34] [35] [36] [37] [38] [39] [40] [41] [42] [43] [44] [45]

Function

SODC_HUMAN Destroys radicals which are normally produced within the cells and which are toxic to biological systems.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

The structural and dynamical properties of the metal-free form of WT human superoxide dismutase 1 (SOD1) and its familial amyotrophic lateral sclerosis (fALS)-related mutants, T54R and I113T, were characterized both in solution, through NMR, and in the crystal, through X-ray diffraction. We found that all 3 X-ray structures show significant structural disorder in 2 loop regions that are, at variance, well defined in the fully-metalated structures. Interestingly, the apo state crystallizes only at low temperatures, whereas all 3 proteins in the metalated form crystallize at any temperature, suggesting that crystallization selects one of the most stable conformations among the manifold adopted by the apo form in solution. Indeed, NMR experiments show that the protein in solution is highly disordered, sampling a large range of conformations. The large conformational variability of the apo state allows the free reduced cysteine Cys-6 to become highly solvent accessible in solution, whereas it is essentially buried in the metalated state and the crystal structures. Such solvent accessibility, together with that of Cys-111, accounts for the tendency to oligomerization of the metal-free state. The present results suggest that the investigation of the solution state coupled with that of the crystal state can provide major insights into SOD1 pathway toward oligomerization in relation to fALS.

Structural and dynamic aspects related to oligomerization of apo SOD1 and its mutants.,Banci L, Bertini I, Boca M, Calderone V, Cantini F, Girotto S, Vieru M Proc Natl Acad Sci U S A. 2009 Apr 28;106(17):6980-5. Epub 2009 Apr 14. PMID:19369197[46]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. ↑ 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. PMID:12963370
  2. ↑ 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. PMID:19741096 doi:10.1091/mbc.E09-02-0112
  3. ↑ 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. PMID:8528216
  4. ↑ 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. PMID:8682505
  5. ↑ 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. PMID:9541385
  6. ↑ 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. PMID:12754496 doi:10.1038/nsb935
  7. ↑ 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. PMID:15056757 doi:10.1073/pnas.0305143101
  8. ↑ 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. Epub 2008 Mar 31. PMID:18378676 doi:http://dx.doi.org/10.1074/jbc.M801522200
  9. ↑ 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. PMID:8446170 doi:http://dx.doi.org/10.1038/362059a0
  10. ↑ 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. PMID:8351519
  11. ↑ 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. PMID:8179602
  12. ↑ 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. PMID:7980516 doi:http://dx.doi.org/10.1006/bbrc.1994.2497
  13. ↑ 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. PMID:8069312
  14. ↑ 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. PMID:7951252
  15. ↑ 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. PMID:7881433
  16. ↑ 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. PMID:7836951
  17. ↑ 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. PMID:7997024
  18. ↑ 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. PMID:7870076 doi:http://dx.doi.org/S0890-8508(84)71046-2
  19. ↑ 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. PMID:7887412
  20. ↑ 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. PMID:7795609
  21. ↑ 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. PMID:7655468
  22. ↑ 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. PMID:7655469
  23. ↑ 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. PMID:7655471
  24. ↑ 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. PMID:7700376 doi:http://dx.doi.org/10.1038/374504a0
  25. ↑ 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. PMID:7647793 doi:http://dx.doi.org/10.1038/ng0595-61
  26. ↑ 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. PMID:7501156
  27. ↑ 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. PMID:7496169
  28. ↑ 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. PMID:8938700
  29. ↑ 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. PMID:8907321
  30. ↑ 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. PMID:8990014 doi:<69::AID-HUMU14>3.0.CO;2-N 10.1002/(SICI)1098-1004(1997)9:1<69::AID-HUMU14>3.0.CO;2-N
  31. ↑ 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. PMID:9101297 doi:<356::AID-HUMU9>3.0.CO;2-3 10.1002/(SICI)1098-1004(1997)9:4<356::AID-HUMU9>3.0.CO;2-3
  32. ↑ 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. PMID:9455977
  33. ↑ 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. PMID:10732812
  34. ↑ 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. PMID:9131652
  35. ↑ 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. PMID:10400992
  36. ↑ 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. PMID:10430435
  37. ↑ 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. PMID:11535232
  38. ↑ 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. PMID:11369193
  39. ↑ 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. PMID:12402272 doi:10.1002/ana.10369
  40. ↑ 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. PMID:12145308 doi:10.1074/jbc.M206559200
  41. ↑ 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. PMID:14506936
  42. ↑ 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. PMID:18552350 doi:10.1074/jbc.M802083200
  43. ↑ 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. PMID:18301754 doi:10.1371/journal.pone.0001677
  44. ↑ 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. PMID:21247266 doi:10.3109/17482968.2011.551939
  45. ↑ 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. PMID:21220647 doi:10.1001/archneurol.2010.352
  46. ↑ Banci L, Bertini I, Boca M, Calderone V, Cantini F, Girotto S, Vieru M. Structural and dynamic aspects related to oligomerization of apo SOD1 and its mutants. Proc Natl Acad Sci U S A. 2009 Apr 28;106(17):6980-5. Epub 2009 Apr 14. PMID:19369197

3ecv, resolution 1.90Å

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