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Volumn 97, Issue 6, 2009, Pages 1709-1718

Structural changes to monomeric CuZn superoxide dismutase caused by the familial amyotrophic lateral sclerosis-associated mutation A4V

Author keywords

[No Author keywords available]

Indexed keywords

COPPER ZINC SUPEROXIDE DISMUTASE; MUTANT PROTEIN; WT1 PROTEIN;

EID: 70350023194     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1016/j.bpj.2009.06.043     Document Type: Article
Times cited : (58)

References (54)
  • 1
    • 33751212177 scopus 로고    scopus 로고
    • Structure, folding, and misfolding of Cu,Zn superoxide dismutase in amyotrophic lateral sclerosis
    • Rakhit, R., and A. Chakrabartty. 2006. Structure, folding, and misfolding of Cu,Zn superoxide dismutase in amyotrophic lateral sclerosis. Biochim. Biophys. Acta. 1762:1025-1037.
    • (2006) Biochim. Biophys. Acta. , vol.1762 , pp. 1025-1037
    • Rakhit, R.1    Chakrabartty, A.2
  • 2
    • 0028815433 scopus 로고
    • Superoxide dismutase is an abundant component in cell bodies, dendrites, and axons of motor neurons and in a subset of other neurons
    • Pardo, C. A., Z. Xu, D. R. Borchelt, D. L. Price, S. S. Sisodia, et al. 1995. Superoxide dismutase is an abundant component in cell bodies, dendrites, and axons of motor neurons and in a subset of other neurons. Proc. Natl. Acad. Sci. USA. 92:954-958.
    • (1995) Proc. Natl. Acad. Sci. USA. , vol.92 , pp. 954-958
    • Pardo, C.A.1    Xu, Z.2    Borchelt, D.R.3    Price, D.L.4    Sisodia, S.S.5
  • 3
    • 0037013224 scopus 로고    scopus 로고
    • Familial amyotrophic lateral sclerosis-associated mutations decrease the thermal stability of distinctly metallated species of human copper/zinc superoxide dismutase
    • Rodriguez, J. A., J. S. Valentine, D. K. Eggers, J. A. Roe, A. Tiwari, et al. 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.
    • (2002) J. Biol. Chem. , vol.277 , pp. 15932-15937
    • Rodriguez, J.A.1    Valentine, J.S.2    Eggers, D.K.3    Roe, J.A.4    Tiwari, A.5
  • 4
    • 0037168643 scopus 로고    scopus 로고
    • Common denominator of Cu/Zn superoxide dismutase mutants associated with amyotrophic lateral sclerosis: Decreased stability of the apo state
    • Lindberg, M. J., L. Tibell, and M. Oliveberg. 2002. Common denominator of Cu/Zn superoxide dismutase mutants associated with amyotrophic lateral sclerosis: decreased stability of the apo state. Proc. Natl. Acad. Sci. USA. 99:16607-16612.
    • (2002) Proc. Natl. Acad. Sci. USA. , vol.99 , pp. 16607-16612
    • Lindberg, M.J.1    Tibell, L.2    Oliveberg, M.3
  • 5
    • 23044431627 scopus 로고    scopus 로고
    • Destabilization of apoprotein is insufficient to explain Cu,Zn-superoxide dismutase-linked ALS pathogenesis
    • Rodriguez, J. A., B. F. Shaw, A. Durazo, S. H. Sohn, P. A. Doucette, et al. 2005. Destabilization of apoprotein is insufficient to explain Cu,Zn-superoxide dismutase-linked ALS pathogenesis. Proc. Natl. Acad. Sci. USA. 102:10516-10521.
    • (2005) Proc. Natl. Acad. Sci. USA. , vol.102 , pp. 10516-10521
    • Rodriguez, J.A.1    Shaw, B.F.2    Durazo, A.3    Sohn, S.H.4    Doucette, P.A.5
  • 6
    • 27644596641 scopus 로고    scopus 로고
    • Opinion: What is the role of protein aggregation in neurodegeneration?
    • Ross, C. A., and M. A. Poirier. 2005. Opinion: what is the role of protein aggregation in neurodegeneration? Nat. Rev. Mol. Cell Biol. 6:891-898.
    • (2005) Nat. Rev. Mol. Cell Biol. , vol.6 , pp. 891-898
    • Ross, C.A.1    Poirier, M.A.2
  • 7
    • 0032544674 scopus 로고    scopus 로고
    • Aggregation and motor neuron toxicity of an ALS-linked SOD1 mutant independent from wild-type SOD1
    • Bruijn, L. I., M. K. Houseweart, S. Kato, K. L. Anderson, S. D. Anderson, et al. 1998. Aggregation and motor neuron toxicity of an ALS-linked SOD1 mutant independent from wild-type SOD1. Science. 281:1851-1854.
    • (1998) Science. , vol.281 , pp. 1851-1854
    • Bruijn, L.I.1    Houseweart, M.K.2    Kato, S.3    Anderson, K.L.4    Anderson, S.D.5
  • 8
    • 0030777650 scopus 로고    scopus 로고
    • Aggregation of mutant Cu/Zn superoxide dismutase proteins in a culture model of ALS
    • Durham, H. D., J. Roy, L. Dong, and D. A. Figlewicz. 1997. Aggregation of mutant Cu/Zn superoxide dismutase proteins in a culture model of ALS. J. Neuropathol. Exp. Neurol. 56:523-530.
    • (1997) J. Neuropathol. Exp. Neurol. , vol.56 , pp. 523-530
    • Durham, H.D.1    Roy, J.2    Dong, L.3    Figlewicz, D.A.4
  • 9
    • 0033749379 scopus 로고    scopus 로고
    • Formation of high molecular weight complexes of mutant Cu, Zn-superoxide dismutase in a mouse model for familial amyotrophic lateral sclerosis
    • Johnston, J. A., M. J. Dalton, M. E. Gurney, and R. R. Kopito. 2000. Formation of high molecular weight complexes of mutant Cu, Zn-superoxide dismutase in a mouse model for familial amyotrophic lateral sclerosis. Proc. Natl. Acad. Sci. USA. 97:12571-12576.
    • (2000) Proc. Natl. Acad. Sci. USA. , vol.97 , pp. 12571-12576
    • Johnston, J.A.1    Dalton, M.J.2    Gurney, M.E.3    Kopito, R.R.4
  • 10
    • 22244479388 scopus 로고    scopus 로고
    • Copper-zinc superoxide dismutase and amyotrophic lateral sclerosis
    • Valentine, J. S., P. A. Doucette, and S. Zittin Potter. 2005. Copper-zinc superoxide dismutase and amyotrophic lateral sclerosis. Annu. Rev. Biochem. 74:563-593.
    • (2005) Annu. Rev. Biochem. , vol.74 , pp. 563-593
    • Valentine, J.S.1    Doucette, P.A.2    Zittin Potter, S.3
  • 12
    • 6344277909 scopus 로고    scopus 로고
    • The rate and equilibrium constants for a multistep reaction sequence for the aggregation of superoxide dismutase in amyotrophic lateral sclerosis
    • Khare, S. D., M. Caplow, and N. V. Dokholyan. 2004. The rate and equilibrium constants for a multistep reaction sequence for the aggregation of superoxide dismutase in amyotrophic lateral sclerosis. Proc. Natl. Acad. Sci. USA. 101:15094-15099.
    • (2004) Proc. Natl. Acad. Sci. USA. , vol.101 , pp. 15094-15099
    • Khare, S.D.1    Caplow, M.2    Dokholyan, N.V.3
  • 13
    • 2442624720 scopus 로고    scopus 로고
    • Monomeric Cu,Zn-superoxide dismutase is a common misfolding intermediate in the oxidation models of sporadic and familial amyotrophic lateral sclerosis
    • Rakhit, R., J. P. Crow, J. R. Lepock, L. H. Kondejewski, N. R. Cashman, et al. 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.
    • (2004) J. Biol. Chem. , vol.279 , pp. 15499-15504
    • Rakhit, R.1    Crow, J.P.2    Lepock, J.R.3    Kondejewski, L.H.4    Cashman, N.R.5
  • 14
    • 2142761528 scopus 로고    scopus 로고
    • An intersubunit disulfide bond prevents in vitro aggregation of a superoxide dismutase-1 mutant linked to familial amytrophic lateral sclerosis
    • Ray, S. S., R. J. Nowak, K. Strokovich, R. H. Brown, Jr., T. Walz, et al. 2004. An intersubunit disulfide bond prevents in vitro aggregation of a superoxide dismutase-1 mutant linked to familial amytrophic lateral sclerosis. Biochemistry. 43:4899-4905.
    • (2004) Biochemistry. , vol.43 , pp. 4899-4905
    • Ray, S.S.1    Nowak, R.J.2    Strokovich, K.3    Brown Jr., R.H.4    Walz, T.5
  • 15
    • 3142621144 scopus 로고    scopus 로고
    • Rings, chains and ladders: Ubiquitin goes to work in the neuron
    • Johnston, J. A., and K. Madura. 2004. Rings, chains and ladders: ubiquitin goes to work in the neuron. Prog. Neurobiol. 73:227-257.
    • (2004) Prog. Neurobiol. , vol.73 , pp. 227-257
    • Johnston, J.A.1    Madura, K.2
  • 16
    • 0035139109 scopus 로고    scopus 로고
    • Cellular defenses against unfolded proteins: A cell biologist thinks about neurodegenerative diseases
    • Sherman, M. Y., and A. L. Goldberg. 2001. Cellular defenses against unfolded proteins: a cell biologist thinks about neurodegenerative diseases. Neuron. 29:15-32.
    • (2001) Neuron. , vol.29 , pp. 15-32
    • Sherman, M.Y.1    Goldberg, A.L.2
  • 17
    • 11144357460 scopus 로고    scopus 로고
    • Dimer destabilization in superoxide dismutase may result in disease-causing properties: Structures of motor neuron disease mutants
    • Hough, M. A., J. G. Grossmann, S. V. Antonyuk, R. W. Strange, P. A. Doucette, et al. 2004. Dimer destabilization in superoxide dismutase may result in disease-causing properties: structures of motor neuron disease mutants. Proc. Natl. Acad. Sci. USA. 101:5976-5981.
    • (2004) Proc. Natl. Acad. Sci. USA. , vol.101 , pp. 5976-5981
    • Hough, M.A.1    Grossmann, J.G.2    Antonyuk, S.V.3    Strange, R.W.4    Doucette, P.A.5
  • 18
    • 0030836641 scopus 로고    scopus 로고
    • The essential dynamics of Cu, Zn superoxide dismutase: Suggestion of intersubunit communication
    • Chillemi, G., M. Falconi, A. Amadei, G. Zimatore, A. Desideri, et al. 1997. The essential dynamics of Cu, Zn superoxide dismutase: suggestion of intersubunit communication. Biophys. J. 73:1007-1018. (Pubitemid 27337636)
    • (1997) Biophysical Journal , vol.73 , Issue.2 , pp. 1007-1018
    • Chillemi, G.1    Falconi, M.2    Amadei, A.3    Zimatore, G.4    Desideri, A.5    Di Nola, A.6
  • 19
    • 0030254837 scopus 로고    scopus 로고
    • Dimer asymmetry in superoxide dismutase studied by molecular dynamics simulation
    • Falconi, M., R. Gallimbeni, and E. Paci. 1996. Dimer asymmetry in superoxide dismutase studied by molecular dynamics simulation. J. Comput. Aided Mol. Des. 10:490-498.
    • (1996) J. Comput. Aided Mol. Des. , vol.10 , pp. 490-498
    • Falconi, M.1    Gallimbeni, R.2    Paci, E.3
  • 21
    • 0242662235 scopus 로고    scopus 로고
    • Folding of Cu, Zn superoxide dismutase and familial amyotrophic lateral sclerosis
    • Khare, S. D., F. Ding, and N. V. Dokholyan. 2003. Folding of Cu, Zn superoxide dismutase and familial amyotrophic lateral sclerosis. J. Mol. Biol. 334:515-525.
    • (2003) J. Mol. Biol. , vol.334 , pp. 515-525
    • Khare, S.D.1    Ding, F.2    Dokholyan, N.V.3
  • 22
    • 34547165170 scopus 로고    scopus 로고
    • Molecular dynamics using atomic-resolution structure reveal structural fluctuations that may lead to polymerization of human Cu-Zn superoxide dismutase
    • Strange, R. W., C. W. Yong, W. Smith, and S. S. Hasnain. 2007. Molecular dynamics using atomic-resolution structure reveal structural fluctuations that may lead to polymerization of human Cu-Zn superoxide dismutase. Proc. Natl. Acad. Sci. USA. 104:10040-10044.
    • (2007) Proc. Natl. Acad. Sci. USA. , vol.104 , pp. 10040-10044
    • Strange, R.W.1    Yong, C.W.2    Smith, W.3    Hasnain, S.S.4
  • 23
    • 33644748183 scopus 로고    scopus 로고
    • Common dynamical signatures of familial amyotrophic lateral sclerosis-associated structurally diverse Cu, Zn superoxide dismutase mutants
    • Khare, S. D., and N. V. Dokholyan. 2006. Common dynamical signatures of familial amyotrophic lateral sclerosis-associated structurally diverse Cu, Zn superoxide dismutase mutants. Proc. Natl. Acad. Sci. USA. 103:3147-3152.
    • (2006) Proc. Natl. Acad. Sci. USA. , vol.103 , pp. 3147-3152
    • Khare, S.D.1    Dokholyan, N.V.2
  • 24
    • 58149402390 scopus 로고    scopus 로고
    • Dynamical roles of metal ions and the disulfide bond in Cu, Zn superoxide dismutase folding and aggregation
    • Ding, F., and N. V. Dokholyan. 2008. Dynamical roles of metal ions and the disulfide bond in Cu, Zn superoxide dismutase folding and aggregation. Proc. Natl. Acad. Sci. USA. 105:19696-19701.
    • (2008) Proc. Natl. Acad. Sci. USA. , vol.105 , pp. 19696-19701
    • Ding, F.1    Dokholyan, N.V.2
  • 25
    • 38049017916 scopus 로고    scopus 로고
    • SOD1A4V-mediated ALS: Absence of a closely linked modifier gene and origination in Asia
    • Broom, W. J., D. V. Johnson, K. E. Auwarter, A. J. Iafrate, C. Russ, et al. 2008. SOD1A4V-mediated ALS: absence of a closely linked modifier gene and origination in Asia. Neurosci. Lett. 430:241-245.
    • (2008) Neurosci. Lett. , vol.430 , pp. 241-245
    • Broom, W.J.1    Johnson, D.V.2    Auwarter, K.E.3    Iafrate, A.J.4    Russ, C.5
  • 26
    • 0037427449 scopus 로고    scopus 로고
    • The structure of holo and metal-deficient wild-type human Cu, Zn superoxide dismutase and its relevance to familial amyotrophic lateral sclerosis
    • Strange, R. W., S. Antonyuk, M. A. Hough, P. A. Doucette, J. A. Rodriguez, et al. 2003. The structure of holo and metal-deficient wild-type human Cu, Zn superoxide dismutase and its relevance to familial amyotrophic lateral sclerosis. J. Mol. Biol. 328:877-891.
    • (2003) J. Mol. Biol. , vol.328 , pp. 877-891
    • Strange, R.W.1    Antonyuk, S.2    Hough, M.A.3    Doucette, P.A.4    Rodriguez, J.A.5
  • 28
    • 0029633167 scopus 로고
    • Potential energy function and parameters for simulations of the molecular dynamics of proteins and nucleic acids in solution
    • Levitt, M., M. Hirshberg, R. Sharon, and V. Daggett. 1995. Potential energy function and parameters for simulations of the molecular dynamics of proteins and nucleic acids in solution. Comput. Phys. Commun. 91:215-231.
    • (1995) Comput. Phys. Commun. , vol.91 , pp. 215-231
    • Levitt, M.1    Hirshberg, M.2    Sharon, R.3    Daggett, V.4
  • 29
    • 0000125216 scopus 로고    scopus 로고
    • Calibration and testing of a water model for simulation of the molecular dynamics of proteins and nucleic acids in solution
    • Levitt, M., M. Hirshberg, R. Sharon, K. E. Laidig, and V. Daggett. 1997. Calibration and testing of a water model for simulation of the molecular dynamics of proteins and nucleic acids in solution. J. Phys. Chem. B. 101:5051-5061.
    • (1997) J. Phys. Chem. B. , vol.101 , pp. 5051-5061
    • Levitt, M.1    Hirshberg, M.2    Sharon, R.3    Laidig, K.E.4    Daggett, V.5
  • 30
    • 12144275299 scopus 로고    scopus 로고
    • Cutoff size need not strongly influence molecular dynamics results for solvated polypeptides
    • Beck, D. A., R. S. Armen, and V. Daggett. 2005. Cutoff size need not strongly influence molecular dynamics results for solvated polypeptides. Biochemistry. 44:609-616.
    • (2005) Biochemistry. , vol.44 , pp. 609-616
    • Beck, D.A.1    Armen, R.S.2    Daggett, V.3
  • 31
    • 3342918929 scopus 로고    scopus 로고
    • Methods for molecular dynamics simulations of protein folding/unfolding in solution
    • DOI 10.1016/j.ymeth.2004.03.008, PII S1046202304000568
    • Beck, D. A., and V. Daggett. 2004. Methods for molecular dynamics simulations of protein folding/unfolding in solution. Methods. 34:112-120. (Pubitemid 38993212)
    • (2004) Methods , vol.34 , Issue.1 , pp. 112-120
    • Beck, D.A.C.1    Daggett, V.2
  • 32
    • 26444534036 scopus 로고    scopus 로고
    • Characterization of a possible amyloidogenic precursor in glutamine-repeat neurodegenerative diseases
    • Armen, R. S., B. M. Bernard, R. Day, D. O. Alonso, and V. Daggett. 2005. Characterization of a possible amyloidogenic precursor in glutamine-repeat neurodegenerative diseases. Proc. Natl. Acad. Sci. USA. 102:13433-13438.
    • (2005) Proc. Natl. Acad. Sci. USA. , vol.102 , pp. 13433-13438
    • Armen, R.S.1    Bernard, B.M.2    Day, R.3    Alonso, D.O.4    Daggett, V.5
  • 33
    • 0009979659 scopus 로고
    • Precise representation of volume properties of water at one atmosphere
    • Kell, G. S. 1967. Precise representation of volume properties of water at one atmosphere. J. Chem. Eng. Data. 12:66-69.
    • (1967) J. Chem. Eng. Data. , vol.12 , pp. 66-69
    • Kell, G.S.1
  • 34
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features
    • Kabsch, W., and C. Sander. 1983. Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features. Biopolymers. 22:2577-2637.
    • (1983) Biopolymers. , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 35
    • 0027325129 scopus 로고
    • Families and the structural relatedness among globular proteins
    • Yee, D. P., and K. A. Dill. 1993. Families and the structural relatedness among globular proteins. Protein Sci. 2:884-899.
    • (1993) Protein Sci. , vol.2 , pp. 884-899
    • Yee, D.P.1    Dill, K.A.2
  • 37
    • 0037013264 scopus 로고    scopus 로고
    • Decreased metallation and activity in subsets of mutant superoxide dismutases associated with familial amyotrophic lateral sclerosis
    • Hayward, L. J., J. A. Rodriguez, J. W. Kim, A. Tiwari, J. J. Goto, et al. 2002. Decreased metallation and activity in subsets of mutant superoxide dismutases associated with familial amyotrophic lateral sclerosis. J. Biol. Chem. 277:15923-15931.
    • (2002) J. Biol. Chem. , vol.277 , pp. 15923-15931
    • Hayward, L.J.1    Rodriguez, J.A.2    Kim, J.W.3    Tiwari, A.4    Goto, J.J.5
  • 38
    • 0030833449 scopus 로고    scopus 로고
    • Decreased zinc affinity of amyotrophic lateral sclerosis-associated superoxide dismutase mutants leads to enhanced catalysis of tyrosine nitration by peroxynitrite
    • Crow, J. P., J. B. Sampson, Y. Zhuang, J. A. Thompson, and J. S. Beckman. 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.
    • (1997) J. Neurochem. , vol.69 , pp. 1936-1944
    • Crow, J.P.1    Sampson, J.B.2    Zhuang, Y.3    Thompson, J.A.4    Beckman, J.S.5
  • 39
    • 11144227941 scopus 로고    scopus 로고
    • Dissociation of human copper-zinc superoxide dismutase dimers using chaotrope and reductant. Insights into the molecular basis for dimer stability
    • Doucette, P. A., L. J. Whitson, X. Cao, V. Schirf, B. Demeler, et al. 2004. Dissociation of human copper-zinc superoxide dismutase dimers using chaotrope and reductant. Insights into the molecular basis for dimer stability. J. Biol. Chem. 279:54558-54566.
    • (2004) J. Biol. Chem. , vol.279 , pp. 54558-54566
    • Doucette, P.A.1    Whitson, L.J.2    Cao, X.3    Schirf, V.4    Demeler, B.5
  • 40
    • 0027965073 scopus 로고
    • Superoxide dismutase 1 with mutations linked to familial amyotrophic lateral sclerosis possesses significant activity
    • Borchelt, D. R., M. K. Lee, H. S. Slunt, M. Guarnieri, Z. S. Xu, et al. 1994. Superoxide dismutase 1 with mutations linked to familial amyotrophic lateral sclerosis possesses significant activity. Proc. Natl. Acad. Sci. USA. 91:8292-8296.
    • (1994) Proc. Natl. Acad. Sci. USA. , vol.91 , pp. 8292-8296
    • Borchelt, D.R.1    Lee, M.K.2    Slunt, H.S.3    Guarnieri, M.4    Xu, Z.S.5
  • 41
    • 34247505040 scopus 로고    scopus 로고
    • Binding of a single zinc ion to one subunit of copper-zinc superoxide dismutase apoprotein substantially influences the structure and stability of the entire homodimeric protein
    • Potter, S. Z., H. Zhu, B. F. Shaw, J. A. Rodriguez, P. A. Doucette, et al. 2007. Binding of a single zinc ion to one subunit of copper-zinc superoxide dismutase apoprotein substantially influences the structure and stability of the entire homodimeric protein. J. Am. Chem. Soc. 129:4575-4583.
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 4575-4583
    • Potter, S.Z.1    Zhu, H.2    Shaw, B.F.3    Rodriguez, J.A.4    Doucette, P.A.5
  • 42
    • 53149103974 scopus 로고    scopus 로고
    • Denaturational stress induces formation of zinc-deficient monomers of cu,zn superoxide dismutase: Implications for pathogenesis in amyotrophic lateral sclerosis
    • Mulligan, V. K., A. Kerman, S. Ho, and A. Chakrabartty. 2008. Denaturational stress induces formation of zinc-deficient monomers of cu,zn superoxide dismutase: implications for pathogenesis in amyotrophic lateral sclerosis. J. Mol. Biol. 383:424-436.
    • (2008) J. Mol. Biol. , vol.383 , pp. 424-436
    • Mulligan, V.K.1    Kerman, A.2    Ho, S.3    Chakrabartty, A.4
  • 43
    • 0029400840 scopus 로고
    • Variable clinical symptoms in familial amyotrophic lateral sclerosis with a novel point mutation in the Cu/Zn superoxide dismutase gene
    • Ikeda, M., K. Abe, M. Aoki, M. Sahara, M. Watanabe, et al. 1995. Variable clinical symptoms in familial amyotrophic lateral sclerosis with a novel point mutation in the Cu/Zn superoxide dismutase gene. Neurology. 45:2038-2042.
    • (1995) Neurology. , vol.45 , pp. 2038-2042
    • Ikeda, M.1    Abe, K.2    Aoki, M.3    Sahara, M.4    Watanabe, M.5
  • 44
    • 34948850962 scopus 로고    scopus 로고
    • Disulfide bond mediates aggregation, toxicity, and ubiquitylation of familial amyotrophic lateral sclerosis-linked mutant SOD1
    • Niwa, J., S. Yamada, S. Ishigaki, J. Sone, M. Takahashi, et al. 2007. Disulfide bond mediates aggregation, toxicity, and ubiquitylation of familial amyotrophic lateral sclerosis-linked mutant SOD1. J. Biol. Chem. 282:28087-28095.
    • (2007) J. Biol. Chem. , vol.282 , pp. 28087-28095
    • Niwa, J.1    Yamada, S.2    Ishigaki, S.3    Sone, J.4    Takahashi, M.5
  • 45
    • 34547415429 scopus 로고    scopus 로고
    • Metal-free superoxide dismutase forms soluble oligomers under physiological conditions: A possible general mechanism for familial ALS
    • Banci, L., I. Bertini, A. Durazo, S. Girotto, E. B. Gralla, 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    Bertini, I.2    Durazo, A.3    Girotto, S.4    Gralla, E.B.5
  • 46
    • 38149115471 scopus 로고    scopus 로고
    • Cysteine 111 affects aggregation and cytotoxicity of mutant Cu,Zn-superoxide dismutase associated with familial amyotrophic lateral sclerosis
    • Cozzolino, M., I. Amori, M. G. Pesaresi, A. Ferri, M. Nencini, et al. 2008. Cysteine 111 affects aggregation and cytotoxicity of mutant Cu,Zn-superoxide dismutase associated with familial amyotrophic lateral sclerosis. J. Biol. Chem. 283:866-874.
    • (2008) J. Biol. Chem. , vol.283 , pp. 866-874
    • Cozzolino, M.1    Amori, I.2    Pesaresi, M.G.3    Ferri, A.4    Nencini, M.5
  • 47
    • 46649096661 scopus 로고    scopus 로고
    • A limited role for disulfide cross-linking in the aggregation of mutant SOD1 linked to familial amyotrophic lateral sclerosis
    • Karch, C. M., and D. R. Borchelt. 2008. A limited role for disulfide cross-linking in the aggregation of mutant SOD1 linked to familial amyotrophic lateral sclerosis. J. Biol. Chem. 283:13528-13537.
    • (2008) J. Biol. Chem. , vol.283 , pp. 13528-13537
    • Karch, C.M.1    Borchelt, D.R.2
  • 48
    • 0037022563 scopus 로고    scopus 로고
    • Natural β-sheet proteins use negative design to avoid edge-to-edge aggregation
    • Richardson, J. S., and D. C. Richardson. 2002. Natural β-sheet proteins use negative design to avoid edge-to-edge aggregation. Proc. Natl. Acad. Sci. USA. 99:2754-2759.
    • (2002) Proc. Natl. Acad. Sci. USA. , vol.99 , pp. 2754-2759
    • Richardson, J.S.1    Richardson, D.C.2
  • 49
    • 33745813117 scopus 로고    scopus 로고
    • Local unfolding in a destabilized, pathogenic variant of superoxide dismutase 1 observed with H/D exchange and mass spectrometry
    • Shaw, B. F., A. Durazo, A. M. Nersissian, J. P. Whitelegge, K. F. Faull, et al. 2006. Local unfolding in a destabilized, pathogenic variant of superoxide dismutase 1 observed with H/D exchange and mass spectrometry. J. Biol. Chem. 281:18167-18176.
    • (2006) J. Biol. Chem. , vol.281 , pp. 18167-18176
    • Shaw, B.F.1    Durazo, A.2    Nersissian, A.M.3    Whitelegge, J.P.4    Faull, K.F.5
  • 50
    • 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., and M. Oliveberg. 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
  • 51
    • 28944435376 scopus 로고    scopus 로고
    • Characterization of two distinct β2-microglobulin unfolding intermediates that may lead to amyloid fibrils of different morphology
    • Armen, R. S., and V. Daggett. 2005. Characterization of two distinct β2-microglobulin unfolding intermediates that may lead to amyloid fibrils of different morphology. Biochemistry. 44:16098-16107.
    • (2005) Biochemistry. , vol.44 , pp. 16098-16107
    • Armen, R.S.1    Daggett, V.2
  • 52
    • 4143067019 scopus 로고    scopus 로고
    • Pauling and Corey's α-pleated sheet structure may define the prefibrillar amyloidogenic intermediate in amyloid disease
    • Armen, R. S., M. L. DeMarco, D. O. Alonso, and V. Daggett. 2004. Pauling and Corey's α-pleated sheet structure may define the prefibrillar amyloidogenic intermediate in amyloid disease. Proc. Natl. Acad. Sci. USA. 101:11622-11627.
    • (2004) Proc. Natl. Acad. Sci. USA. , vol.101 , pp. 11622-11627
    • Armen, R.S.1    Demarco, M.L.2    Alonso, D.O.3    Daggett, V.4
  • 53
    • 4644296906 scopus 로고    scopus 로고
    • Anatomy of an amyloidogenic intermediate: Conversion of β-sheet to α-sheet structure in transthyretin at acidic pH
    • DOI 10.1016/j.str.2004.08.005, PII S0969212604003107
    • Armen, R. S., D. O. Alonso, and V. Daggett. 2004. Anatomy of an amyloidogenic intermediate: conversion of β-sheet to α-sheet structure in transthyretin at acidic pH. Structure. 12:1847-1863. (Pubitemid 39298968)
    • (2004) Structure , vol.12 , Issue.10 , pp. 1847-1863
    • Armen, R.S.1    Alonso, D.O.V.2    Daggett, V.3
  • 54
    • 33749857843 scopus 로고    scopus 로고
    • α-Sheet: The toxic conformer in amyloid diseases?
    • Daggett, V. 2006. α-Sheet: the toxic conformer in amyloid diseases? Acc. Chem. Res. 39:594-602.
    • (2006) Acc. Chem. Res. , vol.39 , pp. 594-602
    • Daggett, V.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.