SOD1‐associated ALS: A promising system for elucidating the origin of protein‐misfolding disease

References

• Aisenbrey , C , Borowik , T , Bystrom , R , Bokvist , M , Lindstrom , F , Misiak , H , Sani , MA and Grobner , G . 2008 . “How is protein aggregation in amyloidogenic diseases modulated by biological membranes?” . Eur. Biophys. J. , 37 : 247 – 255 .
   PubMed Web of Science ®Google Scholar
• Andersen , PM . 2003 . “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. , 4 : 62 – 73 .
   PubMed Web of Science ®Google Scholar
• Assfalg , M , Banci , L , Bertini , I , Turano , P and Vasos , PR . 2003 . “Superoxide dismutase folding/unfolding pathway: role of the metal ions in modulating structural and dynamical features.” . J. Mol. Biol. , 330 : 145 – 158 .
   PubMedGoogle Scholar
• Baglioni , S , Casamenti , F , Bucciantini , M , Luheshi , LM , Taddei , N , Chiti , F , Dobson , CM and Stefani , M . 2006 . “Prefibrillar amyloid aggregates could be generic toxins in higher organisms.” . J. Neurosci. , 26 : 8160 – 8167 .
   PubMed Web of Science ®Google Scholar
• Balch , WE , Morimoto , RI , Dillin , A and Kelly , JW . 2008 . “Adapting proteostasis for disease intervention.” . Science , 319 : 916 – 919 .
   PubMed Web of Science ®Google Scholar
• Banci , L , Bertini , I , Boca , M , Girotto , S , Martinelli , M , Valentine , JS and Vieru , M . 2008 . “SOD1 and amyotrophic lateral sclerosis: mutations and oligomerization.” . PLoS ONE , 3 : e1677
   PubMed Web of Science ®Google Scholar
• Banci , L , Bertini , I , Cantini , F , D'Amelio , N and Gaggelli , E . 2006 . “Human SOD1 before harboring the catalytic metal: solution structure of copper‐depleted, disulfide‐reduced form.” . J. Biol. Chem. , 281 : 2333 – 2337 .
   PubMedGoogle Scholar
• Banci , L , Bertini , I , Cramaro , F , Del Conte , R and Viezzoli , MS . 2003 . “Solution structure of Apo Cu,Zn superoxide dismutase: role of metal ions in protein folding.” . Biochemistry , 42 : 9543 – 9553 .
   PubMed Web of Science ®Google Scholar
• Banci , L , Bertini , I , Durazo , A , Girotto , S , Gralla , EB , Martinelli , M , Valentine , JS , Vieru , M and Whitelegge , JP . 2007 . “Metal‐free superoxide dismutase forms soluble oligomers under physiological conditions: a possible general mechanism for familial ALS.” . Proc. Natl. Acad. Sci. U.S.A. , 104 : 11263 – 11267 .
   PubMedGoogle Scholar
• Bennett , MJ , Choe , S and Eisenberg , D . 1994 . “Domain swapping: entangling alliances between proteins.” . Proc. Natl. Acad. Sci. U.S.A. , 91 : 3127 – 3131 .
   PubMed Web of Science ®Google Scholar
• Bertini , I , Piccioli , M , Viezzoli , MS , Chiu , CY and Mullenbach , GT . 1994 . “A spectroscopic characterization of a monomeric analog of copper, zinc superoxide dismutase.” . Eur. Biophys. J. , 23 : 167 – 176 .
   PubMed Web of Science ®Google Scholar
• Bruijn , LI , Miller , TM and Cleveland , DW . 2004 . “Unraveling the mechanisms involved in motor neuron degeneration in ALS.” . Annu. Rev. Neurosci. , 27 : 723 – 749 .
   PubMed Web of Science ®Google Scholar
• Bryngelson , JD , Onuchic , JN , Socci , ND and Wolynes , PG . 1995 . “Funnels pathways, and the energy landscape of protein folding: a synthesis.” . Proteins , 21 : 167 – 195 .
   PubMed Web of Science ®Google Scholar
• Canet , D , Last , AM , Tito , P , Sunde , M , Spencer , A , Archer , DB , Redfield , C , Robinson , CV and Dobson , CM . 2002 . “Local cooperativity in the unfolding of an amyloidogenic variant of human lysozyme.” . Nat. Struct. Biol. , 9 : 308 – 315 .
   PubMedGoogle Scholar
• Chiti , F , Stefani , M , Taddei , N , Ramponi , G and Dobson , CM . 2003 . “Rationalization of the effects of mutations on peptide and protein aggregation rates.” . Nature (London) , 424 : 805 – 808 .
   PubMed Web of Science ®Google Scholar
• Clarke , J , Cota , E , Fowler , SB and Hamill , SJ . 1999 . “Folding studies of immunoglobulin‐like beta‐sandwich proteins suggest that they share a common folding pathway.” . Folding Des. , 7 : 1145 – 1153 .
   Google Scholar
• Cozzolino , M , Amori , I , Pesaresi , MG , Ferri , A , Nencini , M and Carri , MT . 2008 . “Cysteine 111 affects aggregation and ytotoxicity of mutant Cu,Zn‐superoxide dismutase associated with familial amyotrophic lateral sclerosis.” . J. Biol. Chem. , 283 : 866 – 874 .
   PubMed Web of Science ®Google Scholar
• Crow , JP , Sampson , JB , Zhuang , Y , Thompson , JA and Beckman , JS . 1997 . “Decreased zinc affinity of amyotrophic lateral sclerosis‐associated superoxide dismutase mutants leads to enhanced catalysis of tyrosine nitration by peroxynitrite.” . J. Neurochem. , 69 : 1936 – 1944 .
   PubMed Web of Science ®Google Scholar
• Deng , HX . 1993 . “Amyotrophic lateral sclerosis and structural defects in Cu,Zn superoxide dismutase.” . Science , 261 : 1047 – 1051 .
   PubMed Web of Science ®Google Scholar
• Dickson , D . 2003 . “Neurodegeneration: the molecular pathology of dementia and movement disorders.” . ISN NEUROPATH PRESS .
   Google Scholar
• DiDonato , M . 2003 . “ALS mutants of human superoxide dismutase form fibrous aggregates via framework destabilization.” . J. Mol. Biol. , 332 : 601 – 615 .
   PubMed Web of Science ®Google Scholar
• Dobson , CM . 1999 . “Protein misfolding, evolution and disease.” . Trends Biochem. Sci. , 24 : 329 – 332 .
   PubMed Web of Science ®Google Scholar
• Dunker , AK , Brown , CJ , Lawson , JD , Iakoucheva , LM and Obradovic , Z . 2002 . “Intrinsic disorder and protein function.” . Biochemistry , 41 : 6573 – 6582 .
   PubMed Web of Science ®Google Scholar
• Elam , JS . 2003 . “Amyloid‐like filaments and water‐filled nanotubes formed by SOD1 mutant proteins linked to familial ALS.” . Nat. Struct. Biol. , 10 : 461 – 467 .
   PubMedGoogle Scholar
• Fernandez‐Escamilla , AM , Rousseau , F , Schymkowitz , J and Serrano , L . 2004 . “Prediction of sequence‐dependent and mutational effects on the aggregation of peptides and proteins.” . Nat. Biotechnol. , 22 : 1302 – 1306 .
   PubMed Web of Science ®Google Scholar
• Fersht , AR . 1995 . “Optimization of rates of protein folding: the nucleation‐condensation mechanism and its implications.” . Proc. Natl. Acad. Sci. U.S.A. , 92 : 10869 – 10873 .
   PubMed Web of Science ®Google Scholar
• Fersht , AR . 1999 . Structure and Mechanism in Protein Science: a Guide to Enzyme Catalysis and Protein Folding , New York : WH Freeman and Co. .
   Google Scholar
• Furukawa , Y , Kaneko , K , Yamanaka , K , O'Halloran , TV and Nukina , N . 2008 . “Complete loss of post‐translational modifications triggers fibrillar aggregation of SOD1 in familial form of ALS.” . J. Biol. Chem. , 283 : 24167 – 24176 .
   PubMed Web of Science ®Google Scholar
• Furukawa , Y , Torres , AS and O'Halloran , TV . 2004 . “Oxygen‐induced maturation of SOD1: a key role for disulfide formation by the copper chaperone CCS.” . EMBO J. , 23 : 2872 – 2881 .
   PubMed Web of Science ®Google Scholar
• Giedraitis , V , Sundelof , J , Irizarry , MC , Garevik , N , Hyman , BT , Wahlund , LO , Ingelsson , M and Lannfelt , L . 2007 . “The normal equilibrium between CSF and plasma amyloid beta levels is disrupted in Alzheimer's disease.” . Neurosci. Lett. , 427 : 127 – 131 .
   PubMed Web of Science ®Google Scholar
• Glover , JR , Kowal , AS , Schirmer , EC , Patino , MM , Liu , JJ and Lindquist , S . 1997 . “Self‐seeded fibers formed by Sup35, the protein determinant of [PSI+], a heritable prion‐like factor of S. cerevisiae.” . Cell , 89 : 811 – 819 .
   PubMed Web of Science ®Google Scholar
• Gurney , ME . 1994 . “Motor neuron degeneration in mice that express a human Cu,Zn superoxide dismutase mutation.” . Science , 264 : 1772 – 1775 .
   PubMed Web of Science ®Google Scholar
• Hornberg , A , Logan , DT , Marklund , SL and Oliveberg , M . 2007 . “The coupling between disulphide status, metallation and dimmer interface strength in Cu/Zn superoxide dismutase.” . J. Mol. Biol. , 365 : 333 – 342 .
   PubMed Web of Science ®Google Scholar
• Hough , MA . 2004 . “Dimer destabilization in superoxide dismutase may result in disease‐causing properties: structures of motor neuron disease mutants.” . Proc. Natl. Acad. Sci. U.S.A. , 101 : 5976 – 5981 .
   PubMed Web of Science ®Google Scholar
• Jackson , SE . 1998 . “How do small single‐domain proteins fold?” . Folding Des. , 3 : R81 – R91 .
   PubMedGoogle Scholar
• Jahn , TR and Radford , SE . 2008 . “Folding versus aggregation: polypeptide conformations on competing pathways.” . Arch. Biochem. Biophys. , 469 : 100 – 117 .
   PubMed Web of Science ®Google Scholar
• Joerger , AC and Fersht , AR . 2008 . “Structural biology of the tumor suppressor p53.” . Annu. Rev. Biochem. , 77 : 557 – 582 .
   PubMed Web of Science ®Google Scholar
• Jonsson , PA , Graffmo , KS , Andersen , PM , Brannstrom , T , Lindberg , M , Oliveberg , M and Marklund , SL . 2006 . “Disulphide‐reduced superoxide dismutase‐1 in CNS of transgenic amyotrophic lateral sclerosis models.” . Brain , 129 : 451 – 464 .
   PubMed Web of Science ®Google Scholar
• Khare , SD and Dokholyan , NV . 2006 . “Common dynamical signatures of familial amyotrophic lateral sclerosis‐associated structurally diverse Cu, Zn superoxide dismutase mutants.” . Proc. Natl. Acad. Sci. U.S.A. , 103 : 3147 – 3152 .
   PubMed Web of Science ®Google Scholar
• Lamb , AL , Torres , AS , O'Halloran , TV and Rosenzweig , AC . 2001 . “Heterodimeric structure of superoxide dismutase in complex with its metallochaperone.” . Nat. Struct. Biol. , 8 : 751 – 755 .
   PubMedGoogle Scholar
• Levy , Y , Wolynes , PG and Onuchic , JN . 2004 . “Protein topology determines binding mechanism.” . Proc. Natl. Acad. Sci. U.S.A. , 101 : 511 – 516 .
   PubMed Web of Science ®Google Scholar
• Lindberg , M , Tangrot , J and Oliveberg , M . 2002a . “Complete change of the protein folding transition state upon circular permutation.” . Nat. Struct. Biol. , 9 : 818 – 822 .
   PubMedGoogle Scholar
• Lindberg , MJ , Bystrom , R , Boknas , N , Andersen , PM and Oliveberg , M . 2005 . “Systematically perturbed folding patterns of amyotrophic lateral sclerosis (ALS)‐associated SOD1 mutants.” . Proc. Natl. Acad. Sci. U.S.A. , 102 : 9754 – 9759 .
   PubMed Web of Science ®Google Scholar
• Lindberg , MJ , Normark , J , Holmgren , A and Oliveberg , M . 2004 . “Folding of human superoxide dismutase: disulfide reduction prevents dimerization and produces marginally stable monomers.” . Proc. Natl. Acad. Sci. U.S.A. , 101 : 15893 – 15898 .
   PubMedGoogle Scholar
• Lindberg , MJ , Tibell , L and Oliveberg , M . 2002b . “Common denominator of Cu/Zn superoxide dismutase mutants associated with amyotrophic lateral sclerosis: decreased stability of the apo state.” . Proc. Natl. Acad. Sci. U.S.A. , 99 : 16607 – 16612 .
   PubMed Web of Science ®Google Scholar
• Lindberg , MO , Haglund , E , Hubner , IA , Shakhnovich , EI and Oliveberg , M . 2006 . “Identification of the minimal protein‐folding nucleus through loop‐entropy perturbations.” . Proc. Natl. Acad. Sci. U.S.A. , 103 : 4083 – 4088 .
   PubMedGoogle Scholar
• Liu , Y , Gotte , G , Libonati , M and Eisenberg , D . 2001 . “A domain‐swapped RNase A dimer with implications for amyloid formation.” . Nat. Struct. Biol. , 8 : 211 – 214 .
   PubMedGoogle Scholar
• Lynch , SM , Boswell , SA and Colon , W . 2004 . “Kinetic stability of Cu/Zn superoxide dismutase is dependent on its metal ligands: implications for ALS.” . Biochemistry , 43 : 16525 – 16531 .
   PubMed Web of Science ®Google Scholar
• Lynch , SM and Colon , W . 2006 . “Dominant role of copper in the kinetic stability of Cu/Zn superoxide dismutase.” . Biochem. Biophys. Res. Commun. , 340 : 457 – 461 .
   PubMed Web of Science ®Google Scholar
• McParland , VJ , Kalverda , AP , Homans , SW and Radford , SE . 2002 . “Structural properties of an amyloid precursor of beta(2)‐microglobulin.” . Nat. Struct. Biol. , 9 : 326 – 331 .
   PubMedGoogle Scholar
• Michalik , A and Van Broeckhoven , C . 2003 . “Pathogenesis of polyglutamine disorders: aggregation revisited.” . Hum. Mol. Genet. , 12 : R173 – R186 .
   PubMedGoogle Scholar
• Niwa , J , Yamada , S , Ishigaki , S , Sone , J , Takahashi , M , Katsuno , M , Tanaka , F , Doyu , M and Sobue , G . 2007 . “Disulfide bond mediates aggregation toxicity, and ubiquitylation of familial amyotrophic lateral sclerosis‐linked mutant SOD1.” . J. Biol. Chem. , 282 : 28087 – 28095 .
   PubMed Web of Science ®Google Scholar
• Nordlund , A and Oliveberg , M . 2006 . “Folding of Cu/Zn superoxide dismutase suggests structural hotspots for gain of neurotoxic function in ALS: parallels to precursors in amyloid disease.” . Proc. Natl. Acad. Sci. U.S.A. , 103 : 10218 – 10223 .
   PubMedGoogle Scholar
• Okado‐Matsumoto , A and Fridovich , I . 2002 . “Amyotrophic lateral sclerosis: a proposed mechanism.” . Proc. Natl. Acad. Sci. U.S.A. , 99 : 9010 – 9014 .
   PubMed Web of Science ®Google Scholar
• Oliveberg , M . 1998 . “Alternative explanations for multi‐state kinetics in protein folding: transient aggregation and changeing transition‐state ensambles.” . Acc. Chem. Res. , 31 : 765 – 772 .
   Google Scholar
• Oliveberg , M and Wolynes , PG . 2005 . “The experimental survey of protein‐folding energy landscapes.” . Q. Rev. Biophys. , 38 : 245 – 288 .
   PubMed Web of Science ®Google Scholar
• Otzen , DE , Kristensen , O and Oliveberg , M . 2000 . “Designed protein tetramer zipped together with a hydrophobic Alzheimer homology: a structural clue to amyloid assembly.” . Proc. Natl. Acad. Sci. U.S.A. , 97 : 9907 – 9912 .
   PubMed Web of Science ®Google Scholar
• Otzen , DE and Oliveberg , M . 1999 . “Salt‐induced detour through compact regions of the protein folding landscape [in process citation],” . Proc. Natl. Acad. Sci. U.S.A. , 96 : 11746 – 11751 .
   PubMed Web of Science ®Google Scholar
• Otzen , DE and Oliveberg , M . 2004 . “Transient formation of nano‐crystalline structures during fibrillation of an Abeta‐like peptide.” . Protein Sci. , 13 : 1417 – 1421 .
   PubMedGoogle Scholar
• Platt , GW , McParland , VJ , Kalverda , AP , Homans , SW and Radford , SE . 2005 . “Dynamics in the unfolded state of beta2‐microglobulin studied by NMR.” . J. Mol. Biol. , 346 : 279 – 294 .
   PubMed Web of Science ®Google Scholar
• Plotkin , SS and Onuchic , JN . 2000 . “Investigation of routes and funnels in protein folding by free energy functional methods.” . Proc. Natl. Acad. Sci. U.S.A. , 97 : 6509 – 6514 .
   PubMedGoogle Scholar
• Potter , SZ and Valentine , JS . 2003 . “The perplexing role of copper‐zinc superoxide dismutase in amyotrophic lateral sclerosis (Lou Gehrig's disease).” . JBIC, J. Biol. Inorg. Chem. , 8 : 373 – 380 .
   PubMedGoogle Scholar
• Rakhit , R , Crow , JP , Lepock , JR , Kondejewski , LH , Cashman , NR and Chakrabartty , A . 2004 . “Monomeric Cu,Zn‐superoxide dismutase is a common misfolding intermediate in the oxidation models of sporadic and familial amyotrophic lateral sclerosis.” . J. Biol. Chem. , 279 : 15499 – 15504 .
   PubMed Web of Science ®Google Scholar
• Randles , LG , Lappalainen , I , Fowler , SB , Moore , B , Hamill , SJ and Clarke , J . 2006 . “Using model proteins to quantify the effects of pathogenic mutations in Ig‐like proteins.” . J. Biol. Chem. , 281 : 24216 – 24226 .
   PubMedGoogle Scholar
• Richardson , JS and Richardson , DC . 2002 . “Natural beta ‐sheet proteins use negative design to avoid edge‐to‐edge aggregation.” . Proc. Natl. Acad. Sci. U.S.A. , 99 : 2754 – 2759 .
   PubMed Web of Science ®Google Scholar
• Richardson , JS . 1992 . “Looking at proteins: representations, folding packing, and design.” . Biophys. J. , 63 : 1185 – 1209 .
   PubMedGoogle Scholar
• Ripps , ME , Huntley , GW , Hof , PR , Morrison , JH and Gordon , JW . 1995 . “Transgenic mice expressing an altered murine superoxide dismutase gene provide an animal model of amyotrophic lateral sclerosis.” . Proc. Natl. Acad. Sci. U.S.A. , 92 : 689 – 693 .
   PubMed Web of Science ®Google Scholar
• Roberts , BR , Tainer , JA , Getzoff , ED , Malencik , DA , Anderson , SR , Bomben , VC , Meyers , KR , Karplus , PA and Beckman , JS . 2007 . “Structural characterization of zinc‐deficient human superoxide dismutase and implications for ALS.” . J. Mol. Biol. , 373 : 877 – 890 .
   PubMed Web of Science ®Google Scholar
• Rodriguez , JA , Valentine , JS , Eggers , DK , Roe , JA , Tiwari , A , Brown , RH Jr. and Hayward , LJ . 2002 . “Familial amyotrophic lateral sclerosis‐associated mutations decrease the thermal stability of distinctly metallated species of human copper/zinc superoxide dismutase.” . J. Biol. Chem. , 277 : 15932 – 15937 .
   PubMed Web of Science ®Google Scholar
• Rousseau , F , Schymkowitz , J and Serrano , L . 2006a . “Protein aggregation and amyloidosis: confusion of the kinds?” . Curr. Opin. Struct. Biol. , 16 : 118 – 126 .
   PubMed Web of Science ®Google Scholar
• Rousseau , F , Serrano , L and Schymkowitz , JW . 2006b . “How evolutionary pressure against protein aggregation shaped chaperone specificity.” . J. Mol. Biol. , 355 : 1037 – 1047 .
   PubMed Web of Science ®Google Scholar
• Sandelin , E , Nordlund , A , Andersen , PM , Marklund , SS and Oliveberg , M . 2007 . “Amyotrophic lateral sclerosis‐associated copper/zinc superoxide dismutase mutations preferentially reduce the repulsive charge of the proteins.” . J. Biol. Chem. , 282 : 21230 – 21236 .
   PubMedGoogle Scholar
• Sekijima , Y , Wiseman , RL , Matteson , J , Hammarstrom , P , Miller , SR , Sawkar , AR , Balch , WE and Kelly , JW . 2005 . “The biological and chemical basis for tissue‐selective amyloid disease.” . Cell , 121 : 73 – 85 .
   PubMed Web of Science ®Google Scholar
• Shaw , BF and Valentine , JS . 2007 . “How do ALS‐associated mutations in superoxide dismutase 1 promote aggregation of the protein?” . Trends Biochem. Sci. , 32 : 78 – 85 .
   PubMedGoogle Scholar
• Sherman , MY and Goldberg , AL . 2001 . “Cellular defenses against unfolded proteins: a cell biologist thinks about neurodegenerative diseases.” . Neuron , 29 : 15 – 32 .
   PubMed Web of Science ®Google Scholar
• Silow , M , Tan , YJ , Fersht , AR and Oliveberg , M . 1999 . “Formation of short‐lived protein aggregates directly from the coil in two‐state folding.” . Biochemistry , 38 : 13006 – 13012 .
   PubMedGoogle Scholar
• Silveira , JR , Raymond , GJ , Hughson , AG , Race , RE , Sim , VL , Hayes , SF and Caughey , B . 2005 . “The most infectious prion protein particles.” . Nature (London) , 437 : 257 – 261 .
   PubMed Web of Science ®Google Scholar
• Stathopulos , PB , Rumfeldt , JA , Scholz , GA , Irani , RA , Frey , HE , Hallewell , RA , Lepock , JR and Meiering , EM . 2003 . “Cu/Zn superoxide dismutase mutants associated with amyotrophic lateral sclerosis show enhanced formation of aggregates in vitro.” . Proc. Natl. Acad. Sci. U.S.A. , 100 : 7021 – 7026 .
   PubMed Web of Science ®Google Scholar
• Stroppolo , ME , Malvezzi‐Campeggi , F , Mei , G , Rosato , N and Desideri , A . 2000 . “Role of the tertiary and quaternary structures in the stability of dimeric copper, zinc superoxide dismutases.” . Arch. Biochem. Biophys. , 377 : 215 – 218 .
   PubMed Web of Science ®Google Scholar
• Svensson , AK , Bilsel , O , Kondrashkina , E , Zitzewitz , JA and Matthews , CR . 2006 . “Mapping the folding free energy surface for metal‐free human Cu,Zn superoxide dismutase.” . J. Mol. Biol. , 364 : 1084 – 1102 .
   PubMedGoogle Scholar
• Thirumalai , D , Klimov , DK and Dima , RI . 2003 . “Emerging ideas on the molecular basis of protein and peptide aggregation.” . Curr. Opin. Struct. Biol. , 13 : 146 – 159 .
   PubMed Web of Science ®Google Scholar
• Tiwari , A and Hayward , LJ . 2003 . “Familial amyotrophic lateral sclerosis mutants of copper/zinc superoxide dismutase are susceptible to disulfide reduction.” . J. Biol. Chem. , 278 : 5984 – 5992 .
   PubMed Web of Science ®Google Scholar
• Vande Velde , C , Miller , TM , Cashman , NR and Cleveland , DW . 2008 . “Selective association of misfolded ALS‐linked mutant SOD1 with the cytoplasmic face of mitochondria.” . Proc. Natl. Acad. Sci. U.S.A. , 105 : 4022 – 4027 .
   PubMed Web of Science ®Google Scholar
• Wilczynska , M , Lobov , S , Ohlsson , PI and Ny , T . 2003 . “A redox‐sensitive loop regulates plasminogen activator inhibitor type 2 (PAI‐2) polymerization.” . EMBO J. , 22 : 1753 – 1761 .
   PubMedGoogle Scholar
• Wittung‐Stafshede , P . 2004 . “Role of cofactors in folding of the blue‐copper protein azurin.” . Inorg. Chem. , 43 : 7926 – 7933 .
   PubMedGoogle Scholar
• Yang , S , Cho , SS , Levy , Y , Cheung , MS , Levine , H , Wolynes , PG and Onuchic , JN . 2004 . “Domain swapping is a consequence of minimal frustration.” . Proc. Natl. Acad. Sci. U.S.A. , 101 : 13786 – 13791 .
   PubMedGoogle Scholar
• Zetterstrom , P , Stewart , HG , Bergemalm , D , Jonsson , PA , Graffmo , KS , Andersen , PM , Brannstrom , T , Oliveberg , M and Marklund , SL . 2007 . “Soluble misfolded subfractions of mutant superoxide dismutase‐1s are enriched in spinal cords throughout life in murine ALS models.” . Proc. Natl. Acad. Sci. U.S.A. , 104 : 14157 – 14162 .
   PubMedGoogle Scholar
• Zhang , F , Strom , AL , Fukada , K , Lee , S , Hayward , LJ and Zhu , H . 2007 . “Interaction between familial amyotrophic lateral sclerosis (ALS)‐linked SOD1 mutants and the dynein complex.” . J. Biol. Chem. , 282 : 16691 – 16699 .
   PubMedGoogle Scholar