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Volumn 109, Issue 44, 2012, Pages 17868-17873

Fibrillation precursor of superoxide dismutase 1 revealed by gradual tuning of the protein-folding equilibrium

Author keywords

[No Author keywords available]

Indexed keywords

COPPER ZINC SUPEROXIDE DISMUTASE;

EID: 84868142104     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1201795109     Document Type: Article
Times cited : (59)

References (43)
  • 2
    • 7244256224 scopus 로고    scopus 로고
    • Sonication of proteins causes formation of aggregates that resemble amyloid
    • Stathopulos PB, et al. (2004) Sonication of proteins causes formation of aggregates that resemble amyloid. Protein Sci 13:3017-3027.
    • (2004) Protein Sci , vol.13 , pp. 3017-3027
    • Stathopulos, P.B.1
  • 3
    • 53049109088 scopus 로고    scopus 로고
    • Complete loss of post-translational modifications triggers fibrillar aggregation of SOD1 in familial form of ALS
    • Furukawa Y, Kaneko K, Yamanaka K, O'Halloran TV, 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.
    • (2008) J Biol Chem , vol.283 , pp. 24167-24176
    • Furukawa, Y.1    Kaneko, K.2    Yamanaka, K.3    O'Halloran, T.V.4    Nukina, N.5
  • 4
    • 57749100302 scopus 로고    scopus 로고
    • Initiation and elongation in fibrillation of ALS-linked superoxide dismutase
    • Chattopadhyay M, et al. (2008) Initiation and elongation in fibrillation of ALS-linked superoxide dismutase. Proc Natl Acad Sci USA 105:18663-18668.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 18663-18668
    • Chattopadhyay, M.1
  • 5
    • 79959887638 scopus 로고    scopus 로고
    • A diversity of assembly mechanisms of a generic amyloid fold
    • Eichner T, Radford SE (2011) A diversity of assembly mechanisms of a generic amyloid fold. Mol Cell 43:8-18.
    • (2011) Mol Cell , vol.43 , pp. 8-18
    • Eichner, T.1    Radford, S.E.2
  • 6
    • 77954586762 scopus 로고    scopus 로고
    • Mutation-dependent polymorphism of Cu,Zn-superoxide dismutase aggregates in the familial form of amyotrophic lateral sclerosis
    • Furukawa Y, Kaneko K, Yamanaka K, Nukina N (2010) Mutation-dependent polymorphism of Cu,Zn-superoxide dismutase aggregates in the familial form of amyotrophic lateral sclerosis. J Biol Chem 285:22221-22231.
    • (2010) J Biol Chem , vol.285 , pp. 22221-22231
    • Furukawa, Y.1    Kaneko, K.2    Yamanaka, K.3    Nukina, N.4
  • 7
    • 0037795635 scopus 로고    scopus 로고
    • Cu/Zn superoxide dismutase mutants associated with amyotrophic lateral sclerosis show enhanced formation of aggregates in vitro
    • Stathopulos PB, et al. (2003) Cu/Zn superoxide dismutase mutants associated with amyotrophic lateral sclerosis show enhanced formation of aggregates in vitro. Proc Natl Acad Sci USA 100:7021-7026.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 7021-7026
    • Stathopulos, P.B.1
  • 8
    • 78650294951 scopus 로고    scopus 로고
    • Lipid molecules induce the cytotoxic aggregation of Cu/Zn superoxide dismutase with structurally disordered regions
    • Choi I, et al. (2011) Lipid molecules induce the cytotoxic aggregation of Cu/Zn superoxide dismutase with structurally disordered regions. BiochimBiophys Acta 1812:41-48.
    • (2011) BiochimBiophys Acta , vol.1812 , pp. 41-48
    • Choi, I.1
  • 9
    • 34547415429 scopus 로고    scopus 로고
    • Metal-free superoxide dismutase forms soluble oligomers under physiological conditions: A possible general mechanism for familial ALS
    • Banci L, et al. (2007) Metal-free superoxide dismutase forms soluble oligomers under physiological conditions: A possible general mechanism for familial ALS. Proc Natl Acad Sci USA 104:11263-11267.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 11263-11267
    • Banci, L.1
  • 10
    • 78650635303 scopus 로고    scopus 로고
    • Nonamyloid aggregates arising from mature copper/zinc superoxide dismutases resemble those observed in amyotrophic lateral sclerosis
    • Hwang YM, et al. (2010) Nonamyloid aggregates arising from mature copper/zinc superoxide dismutases resemble those observed in amyotrophic lateral sclerosis. J Biol Chem 285:41701-41711.
    • (2010) J Biol Chem , vol.285 , pp. 41701-41711
    • Hwang, Y.M.1
  • 11
    • 33846678063 scopus 로고    scopus 로고
    • How do ALS-associated mutations in superoxide dismutase 1 promote aggregation of the protein
    • Shaw BF, Valentine JS (2007) How do ALS-associated mutations in superoxide dismutase 1 promote aggregation of the protein? Trends Biochem Sci 32:78-85
    • (2007) Trends Biochem Sci , vol.32 , pp. 78-85
    • Shaw, B.F.1    Valentine, J.S.2
  • 12
    • 77957128218 scopus 로고    scopus 로고
    • Folding catalysis by transient coordination of Zn2+ to the Cu ligands of the ALS-associated enzyme Cu/Zn superoxide dismutase 1
    • Leinartaite L, Saraboji K, Nordlund A, Logan DT, Oliveberg M (2010) Folding catalysis by transient coordination of Zn2+ to the Cu ligands of the ALS-associated enzyme Cu/Zn superoxide dismutase 1. J Am Chem Soc 132:13495-13504.
    • (2010) J Am Chem Soc , vol.132 , pp. 13495-13504
    • Leinartaite, L.1    Saraboji, K.2    Nordlund, A.3    Logan, D.T.4    Oliveberg, M.5
  • 13
    • 80053596817 scopus 로고    scopus 로고
    • Understanding the complex mechanisms of beta2-microglobulin amyloid assembly
    • Eichner T, Radford SE (2011) Understanding the complex mechanisms of beta2-microglobulin amyloid assembly. FEBS J 278:3868-3883.
    • (2011) FEBS J , vol.278 , pp. 3868-3883
    • Eichner, T.1    Radford, S.E.2
  • 14
    • 0037058942 scopus 로고    scopus 로고
    • Sequencedependent denaturation energetics: A major determinant in amyloid disease diversity
    • Hammarstrom P, Jiang X, Hurshman AR, Powers ET, Kelly JW (2002) Sequencedependent denaturation energetics: A major determinant in amyloid disease diversity. Proc Natl Acad Sci USA 4(99 Suppl.):16427-16432.
    • (2002) Proc Natl Acad Sci USA , vol.4 , Issue.99 SUPPL. , pp. 16427-16432
    • Hammarstrom, P.1    Jiang, X.2    Hurshman, A.R.3    Powers, E.T.4    Kelly, J.W.5
  • 15
    • 0042736853 scopus 로고    scopus 로고
    • ALS mutants of human superoxide dismutase form fibrous aggregates via framework destabilization
    • DiDonato M, et al. (2003) ALS mutants of human superoxide dismutase form fibrous aggregates via framework destabilization. J Mol Biol 332:601-615.
    • (2003) J Mol Biol , vol.332 , pp. 601-615
    • Didonato, M.1
  • 16
    • 70849113863 scopus 로고    scopus 로고
    • Transient structural distortion of metal-free Cu/Zn superoxide dismutase triggers aberrant oligomerization
    • Teilum K, et al. (2009) Transient structural distortion of metal-free Cu/Zn superoxide dismutase triggers aberrant oligomerization. Proc Natl Acad Sci USA 106:18273-18278.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 18273-18278
    • Teilum, K.1
  • 17
    • 0038442784 scopus 로고    scopus 로고
    • Amyloid-like filaments and water-filled nanotubes formed by SOD1 mutant proteins linked to familial ALS
    • Elam JS, et al. (2003) Amyloid-like filaments and water-filled nanotubes formed by SOD1 mutant proteins linked to familial ALS. Nat Struct Biol 10:461-467.
    • (2003) Nat Struct Biol , vol.10 , pp. 461-467
    • Elam, J.S.1
  • 18
    • 22244489417 scopus 로고    scopus 로고
    • Systematically perturbed folding patterns of amyotrophic lateral sclerosis (ALS)-associated SOD1 mutants
    • Lindberg MJ, Bystrom R, Boknas N, Andersen PM, Oliveberg M (2005) Systematically perturbed folding patterns of amyotrophic lateral sclerosis (ALS)-associated SOD1 mutants. Proc Natl Acad Sci USA 102:9754-9759.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 9754-9759
    • Lindberg, M.J.1    Bystrom, R.2    Boknas, N.3    Andersen, P.M.4    Oliveberg, M.5
  • 19
    • 67649852607 scopus 로고    scopus 로고
    • Functional features cause misfolding of the ALS-provoking enzyme SOD1
    • Nordlund A, et al. (2009) Functional features cause misfolding of the ALS-provoking enzyme SOD1. Proc Natl Acad Sci USA 106:9667-9672.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 9667-9672
    • Nordlund, A.1
  • 20
    • 77957021146 scopus 로고    scopus 로고
    • Aggregation modulating elements in mutant human superoxide dismutase 1
    • Karch CM, Borchelt DR (2010) Aggregation modulating elements in mutant human superoxide dismutase 1. Arch Biochem Biophys 503:175-182.
    • (2010) Arch Biochem Biophys , vol.503 , pp. 175-182
    • Karch, C.M.1    Borchelt, D.R.2
  • 21
    • 33745889333 scopus 로고    scopus 로고
    • Folding of Cu/Zn superoxide dismutase suggests structural hotspots for gain of neurotoxic function in ALS: Parallels to precursors in amyloid disease
    • Nordlund A, OlivebergM(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 USA 103:10218-10223.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 10218-10223
    • Nordlund, A.1    Oliveberg, M.2
  • 22
    • 8644290067 scopus 로고    scopus 로고
    • Folding of human superoxide dismutase: Disulfide reduction prevents dimerization and produces marginally stable monomers
    • Lindberg MJ, Normark J, Holmgren A, Oliveberg M (2004) Folding of human superoxide dismutase: Disulfide reduction prevents dimerization and produces marginally stable monomers. Proc Natl Acad Sci USA 101:15893-15898.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 15893-15898
    • Lindberg, M.J.1    Normark, J.2    Holmgren, A.3    Oliveberg, M.4
  • 23
    • 80053020591 scopus 로고    scopus 로고
    • Cutting off functional loops from homodimeric enzyme superoxide dismutase 1 (SOD1) leaves monomeric beta-barrels
    • Danielsson J, Kurnik M, Lang L, Oliveberg M (2011) Cutting off functional loops from homodimeric enzyme superoxide dismutase 1 (SOD1) leaves monomeric beta-barrels. J Biol Chem 286:33070-33083.
    • (2011) J Biol Chem , vol.286 , pp. 33070-33083
    • Danielsson, J.1    Kurnik, M.2    Lang, L.3    Oliveberg, M.4
  • 24
    • 0028856785 scopus 로고
    • Optimization of rates of protein folding: The nucleation-condensation mechanism and its implications
    • Fersht AR (1995) Optimization of rates of protein folding: The nucleation-condensation mechanism and its implications. Proc Natl Acad Sci USA 92:10869-10873.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 10869-10873
    • Fersht, A.R.1
  • 25
    • 33751071644 scopus 로고    scopus 로고
    • Mapping the folding free energy surface for metal-free human Cu,Zn superoxide dismutase
    • Svensson AK, Bilsel O, Kondrashkina E, Zitzewitz JA, Matthews CR (2006) Mapping the folding free energy surface for metal-free human Cu,Zn superoxide dismutase. J Mol Biol 364:1084-1102.
    • (2006) J Mol Biol , vol.364 , pp. 1084-1102
    • Svensson, A.K.1    Bilsel, O.2    Kondrashkina, E.3    Zitzewitz, J.A.4    Matthews, C.R.5
  • 27
    • 33750826280 scopus 로고    scopus 로고
    • General structural motifs of amyloid protofilaments
    • Ferguson N, et al. (2006) General structural motifs of amyloid protofilaments. Proc Natl Acad Sci USA 103:16248-16253.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 16248-16253
    • Ferguson, N.1
  • 28
    • 23444445907 scopus 로고    scopus 로고
    • Competing pathways determine fibril morphology in the self-assembly of beta2-microglobulin into amyloid
    • Gosal WS, et al. (2005) Competing pathways determine fibril morphology in the self-assembly of beta2-microglobulin into amyloid. J Mol Biol 351:850-864.
    • (2005) J Mol Biol , vol.351 , pp. 850-864
    • Gosal, W.S.1
  • 29
    • 0036784667 scopus 로고    scopus 로고
    • A kinetic study of beta-lactoglobulin amyloid fibril formation promoted by urea
    • Hamada D, Dobson CM (2002) A kinetic study of beta-lactoglobulin amyloid fibril formation promoted by urea. Protein Sci 11:2417-2426.
    • (2002) Protein Sci , vol.11 , pp. 2417-2426
    • Hamada, D.1    Dobson, C.M.2
  • 30
    • 72149118250 scopus 로고    scopus 로고
    • An analytical solution to the kinetics of breakable filament assembly
    • Knowles TP, et al. (2009) An analytical solution to the kinetics of breakable filament assembly. Science 326:1533-1537.
    • (2009) Science , vol.326 , pp. 1533-1537
    • Knowles, T.P.1
  • 31
    • 48249092311 scopus 로고    scopus 로고
    • Systematic analysis of nucleation-dependent polymerization reveals new insights into the mechanism of amyloid self-assembly
    • Xue WF, Homans SW, Radford SE (2008) Systematic analysis of nucleation-dependent polymerization reveals new insights into the mechanism of amyloid self-assembly. Proc Natl Acad Sci USA 105:8926-8931.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 8926-8931
    • Xue, W.F.1    Homans, S.W.2    Radford, S.E.3
  • 32
    • 0032877134 scopus 로고    scopus 로고
    • Analysis of protein aggregation kinetics
    • Ferrone F (1999) Analysis of protein aggregation kinetics. Methods Enzymol 309:256-274.
    • (1999) Methods Enzymol , vol.309 , pp. 256-274
    • Ferrone, F.1
  • 33
    • 0037397705 scopus 로고    scopus 로고
    • Emerging ideas on the molecular basis of protein and peptide aggregation
    • Thirumalai D, Klimov DK, Dima RI (2003) Emerging ideas on the molecular basis of protein and peptide aggregation. Curr Opin Struct Biol 13:146-159.
    • (2003) Curr Opin Struct Biol , vol.13 , pp. 146-159
    • Thirumalai, D.1    Klimov, D.K.2    Dima, R.I.3
  • 34
    • 65249099497 scopus 로고    scopus 로고
    • Fundamental aspects of protein-protein association kinetics
    • Schreiber G, Haran G, Zhou HX (2009) Fundamental aspects of protein-protein association kinetics. Chem Rev 109:839-860.
    • (2009) Chem Rev , vol.109 , pp. 839-860
    • Schreiber, G.1    Haran, G.2    Zhou, H.X.3
  • 35
    • 84857031320 scopus 로고    scopus 로고
    • Dynamics and mechanisms of coupled protein folding and binding reactions
    • Kiefhaber T, Bachmann A, Jensen KS (2012) Dynamics and mechanisms of coupled protein folding and binding reactions. Curr Opin Struct Biol 22:21-29.
    • (2012) Curr Opin Struct Biol , vol.22 , pp. 21-29
    • Kiefhaber, T.1    Bachmann, A.2    Jensen, K.S.3
  • 36
    • 0034255123 scopus 로고    scopus 로고
    • Speedingmolecular recognition by using the folding funnel: The fly-casting mechanism
    • Shoemaker BA, Portman JJ,Wolynes PG (2000) Speedingmolecular recognition by using the folding funnel: The fly-casting mechanism. Proc Natl Acad Sci USA 97:8868-8873.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 8868-8873
    • Shoemaker, B.A.1    Portman, J.J.2    Wolynes, P.G.3
  • 37
    • 79952741171 scopus 로고    scopus 로고
    • Mapping backbone and side-chain interactions in the transition state of a coupled protein folding and binding reaction
    • Bachmann A, Wildemann D, Praetorius F, Fischer G, Kiefhaber T (2011) Mapping backbone and side-chain interactions in the transition state of a coupled protein folding and binding reaction. Proc Natl Acad Sci USA 108:3952-3957.
    • (2011) Proc Natl Acad Sci USA , vol.108 , pp. 3952-3957
    • Bachmann, A.1    Wildemann, D.2    Praetorius, F.3    Fischer, G.4    Kiefhaber, T.5
  • 38
    • 0042467550 scopus 로고    scopus 로고
    • Rationalization of the effects of mutations on peptide and protein aggregation rates
    • Chiti F, Stefani M, Taddei N, Ramponi G, Dobson CM (2003) Rationalization of the effects of mutations on peptide and protein aggregation rates. Nature 424:805-808.
    • (2003) Nature , vol.424 , pp. 805-808
    • Chiti, F.1    Stefani, M.2    Taddei, N.3    Ramponi, G.4    Dobson, C.M.5
  • 39
    • 0034730203 scopus 로고    scopus 로고
    • Designed protein tetramer zipped together with a hydrophobic Alzheimer homology: A structural clue to amyloid assembly
    • Otzen DE, Kristensen O, Oliveberg M (2000) Designed protein tetramer zipped together with a hydrophobic Alzheimer homology: A structural clue to amyloid assembly. Proc Natl Acad Sci USA 97:9907-9912.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 9907-9912
    • Otzen, D.E.1    Kristensen, O.2    Oliveberg, M.3
  • 40
    • 67651183838 scopus 로고    scopus 로고
    • Position-dependent electrostatic protection against protein aggregation
    • Buell AK, et al. (2009) Position-dependent electrostatic protection against protein aggregation. Chembiochem 10:1309-1312.
    • (2009) Chembiochem , vol.10 , pp. 1309-1312
    • Buell, A.K.1
  • 41
    • 77955352066 scopus 로고    scopus 로고
    • Novel antibodies reveal inclusions containing non-native SOD1 in sporadic ALS patients
    • Forsberg K, et al. (2010) Novel antibodies reveal inclusions containing non-native SOD1 in sporadic ALS patients. PLoS One 5:e11552.
    • (2010) PLoS One , vol.5
    • Forsberg, K.1
  • 42
    • 77949278013 scopus 로고    scopus 로고
    • Fibril fragmentation in amyloid assembly and cytotoxicity: When size matters
    • Xue WF, Hellewell AL, Hewitt EW, Radford SE (2010) Fibril fragmentation in amyloid assembly and cytotoxicity: When size matters. Prion 4:20-25.
    • (2010) Prion , vol.4 , pp. 20-25
    • Xue, W.F.1    Hellewell, A.L.2    Hewitt, E.W.3    Radford, S.E.4
  • 43
    • 34547120448 scopus 로고    scopus 로고
    • Amyotrophic lateral sclerosis-associated copper/zinc superoxide dismutase mutations preferentially reduce the repulsive charge of the proteins
    • Sandelin E, Nordlund A, Andersen PM, Marklund SS, 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.
    • (2007) J Biol Chem , vol.282 , pp. 21230-21236
    • Sandelin, E.1    Nordlund, A.2    Andersen, P.M.3    Marklund, S.S.4    Oliveberg, M.5


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