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Volumn 52, Issue 36, 2013, Pages 6145-6150

Structural consequences of cysteinylation of Cu/Zn-superoxide dismutase

Author keywords

[No Author keywords available]

Indexed keywords

CONFORMATIONAL CHANGE; CU/ZN-SUPEROXIDE DISMUTASE; DIMER INTERFACE; DNA DAMAGES; METALLOENZYMES; PROTEIN CONFORMATIONAL CHANGES; SUPEROXIDE ANIONS; THREE-DIMENSIONAL STRUCTURE;

EID: 84884234335     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi400613h     Document Type: Article
Times cited : (26)

References (34)
  • 1
    • 0014410114 scopus 로고
    • The reduction of cytochrome c by milk xanthine oxidase
    • McCord, J. M. and Fridovich, I. (1968) The reduction of cytochrome c by milk xanthine oxidase J. Biol. Chem 243, 5753-5760
    • (1968) J. Biol. Chem , vol.243 , pp. 5753-5760
    • McCord, J.M.1    Fridovich, I.2
  • 2
    • 3543055852 scopus 로고    scopus 로고
    • Direct Probing of Copper Active Site and Free Radical Formed during Bicarbonate-dependent Peroxidase Activity of Bovine and Human Copper,Zinc-superoxide Dismutases: Low-Temperature Electron Paramagnetic Resonance and Electron Nuclear Double Resonance Studies
    • Karunakaran, C., Zhang, H., Crow, J. P., Antholine, W. E., and Kalyanaraman, B. (2004) Direct Probing of Copper Active Site and Free Radical Formed during Bicarbonate-dependent Peroxidase Activity of Bovine and Human Copper,Zinc-superoxide Dismutases: Low-Temperature Electron Paramagnetic Resonance and Electron Nuclear Double Resonance Studies J. Biol. Chem. 279, 32534-32540
    • (2004) J. Biol. Chem. , vol.279 , pp. 32534-32540
    • Karunakaran, C.1    Zhang, H.2    Crow, J.P.3    Antholine, W.E.4    Kalyanaraman, B.5
  • 3
    • 0037929802 scopus 로고    scopus 로고
    • Bicarbonate-dependent peroxidase activity of human Cu,Zn-superoxide dismutase induces covalent aggregation of protein: Intermediacy of tryptophan-derived oxidation products
    • Zhang, H., Andrekopoulos, C., Joseph, J., Chandran, K., Karoui, H., Crow, J. P., and Kalyanaraman, B. (2003) Bicarbonate-dependent peroxidase activity of human Cu,Zn-superoxide dismutase induces covalent aggregation of protein: intermediacy of tryptophan-derived oxidation products J. Biol. Chem. 278, 24078-24089
    • (2003) J. Biol. Chem. , vol.278 , pp. 24078-24089
    • Zhang, H.1    Andrekopoulos, C.2    Joseph, J.3    Chandran, K.4    Karoui, H.5    Crow, J.P.6    Kalyanaraman, B.7
  • 5
    • 0029050058 scopus 로고
    • Subunit-destabilizing mutations in Drosophila copper/zinc superoxide dismutase: Neuropathology and a model of dimer dysequilibrium
    • Phillips, J. P., Tainer, J. A., Getzoff, E. D., Boulianne, G. L., Kirby, K., and Hilliker, A. J. (1995) Subunit-destabilizing mutations in Drosophila copper/zinc superoxide dismutase: neuropathology and a model of dimer dysequilibrium Proc. Natl. Acad. Sci. U. S. A. 92, 8574-8578
    • (1995) Proc. Natl. Acad. Sci. U. S. A. , vol.92 , pp. 8574-8578
    • Phillips, J.P.1    Tainer, J.A.2    Getzoff, E.D.3    Boulianne, G.L.4    Kirby, K.5    Hilliker, A.J.6
  • 6
    • 15444379991 scopus 로고    scopus 로고
    • Increased spontaneous DNA damage in Cu/Zn superoxide dismutase (SOD1) deficient Drosophila
    • Woodruff, R. C., Phillips, J. P., and Hilliker, A. J. (2004) Increased spontaneous DNA damage in Cu/Zn superoxide dismutase (SOD1) deficient Drosophila Genome 47, 1029-1035
    • (2004) Genome , vol.47 , pp. 1029-1035
    • Woodruff, R.C.1    Phillips, J.P.2    Hilliker, A.J.3
  • 7
    • 26844568877 scopus 로고    scopus 로고
    • Characterization of cysteinylation of pharmaceutical-grade human serum albumin by electrospray ionization mass spectrometry and low-energy collision-induced dissociation tandem mass spectrometry
    • Kleinova, M., Belgacem, O., Pock, K., Rizzi, A., Buchacher, A., and Allmaier, G. (2005) Characterization of cysteinylation of pharmaceutical-grade human serum albumin by electrospray ionization mass spectrometry and low-energy collision-induced dissociation tandem mass spectrometry RCM 19, 2965-2973
    • (2005) RCM , vol.19 , pp. 2965-2973
    • Kleinova, M.1    Belgacem, O.2    Pock, K.3    Rizzi, A.4    Buchacher, A.5    Allmaier, G.6
  • 8
    • 0035423710 scopus 로고    scopus 로고
    • Identification and location of a cysteinyl posttranslational modification in an amyloidogenic kappa1 light chain protein by electrospray ionization and matrix-assisted laser desorption/ionization mass spectrometry
    • Lim, A., Wally, J., Walsh, M. T., Skinner, M., and Costello, C. E. (2001) Identification and location of a cysteinyl posttranslational modification in an amyloidogenic kappa1 light chain protein by electrospray ionization and matrix-assisted laser desorption/ionization mass spectrometry Anal. Biochem. 295, 45-56
    • (2001) Anal. Biochem. , vol.295 , pp. 45-56
    • Lim, A.1    Wally, J.2    Walsh, M.T.3    Skinner, M.4    Costello, C.E.5
  • 9
    • 34548819035 scopus 로고    scopus 로고
    • S-cysteinylation is a general mechanism for thiol protection of Bacillus subtilis proteins after oxidative stress
    • Hochgrafe, F., Mostertz, J., Pother, D. C., Becher, D., Helmann, J. D., and Hecker, M. (2007) S-cysteinylation is a general mechanism for thiol protection of Bacillus subtilis proteins after oxidative stress J. Biol. Chem. 282, 25981-25985
    • (2007) J. Biol. Chem. , vol.282 , pp. 25981-25985
    • Hochgrafe, F.1    Mostertz, J.2    Pother, D.C.3    Becher, D.4    Helmann, J.D.5    Hecker, M.6
  • 10
    • 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., Whitson, L. J., Cao, X., Schirf, V., Demeler, B., Valentine, J. S., Hansen, J. C., and Hart, P. J. (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    Valentine, J.S.6    Hansen, J.C.7    Hart, P.J.8
  • 11
    • 0037013264 scopus 로고    scopus 로고
    • Decreased metallation and activity in subsets of mutant superoxide dismutases associated with familial amyotrophic lateral sclerosis
    • Hayward, L. J., Rodriguez, J. A., Kim, J. W., Tiwari, A., Goto, J. J., Cabelli, D. E., Valentine, J. S., and Brown, R. H., Jr. (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    Cabelli, D.E.6    Valentine, J.S.7    Brown Jr., R.H.8
  • 12
    • 78650733738 scopus 로고    scopus 로고
    • Strategies for stabilizing superoxide dismutase (SOD1), the protein destabilized in the most common form of familial amyotrophic lateral sclerosis
    • Auclair, J. R., Boggio, K. J., Petsko, G. A., Ringe, D., and Agar, J. N. (2010) Strategies for stabilizing superoxide dismutase (SOD1), the protein destabilized in the most common form of familial amyotrophic lateral sclerosis Proc. Natl. Acad. Sci. U. S. A. 107, 21394-21399
    • (2010) Proc. Natl. Acad. Sci. U. S. A. , vol.107 , pp. 21394-21399
    • Auclair, J.R.1    Boggio, K.J.2    Petsko, G.A.3    Ringe, D.4    Agar, J.N.5
  • 13
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski, Z. and Minor, W. (1997) Processing of X-ray diffraction data collected in oscillation mode Methods Enzymol. 276, 307-326
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 14
    • 0037779022 scopus 로고    scopus 로고
    • A statistic for local intensity differences: Robustness to anisotropy and pseudo-centering and utility for detecting twinning
    • Padilla, J. E. and Yeates, T. O. (2003) A statistic for local intensity differences: robustness to anisotropy and pseudo-centering and utility for detecting twinning Acta Crystallogr., Sect. D: Biol. Crystallogr. 59, 1124-1130
    • (2003) Acta Crystallogr., Sect. D: Biol. Crystallogr. , vol.59 , pp. 1124-1130
    • Padilla, J.E.1    Yeates, T.O.2
  • 17
    • 33744459472 scopus 로고    scopus 로고
    • Toward the structural genomics of complexes: Crystal structure of a PE/PPE protein complex from Mycobacterium tuberculosis
    • Strong, M., Sawaya, M. R., Wang, S. S., Phillips, M., Cascio, D., and Eisenberg, D. (2006) Toward the structural genomics of complexes: Crystal structure of a PE/PPE protein complex from Mycobacterium tuberculosis Proc. Natl. Acad. Sci. U. S. A. 103, 8060-8065
    • (2006) Proc. Natl. Acad. Sci. U. S. A. , vol.103 , pp. 8060-8065
    • Strong, M.1    Sawaya, M.R.2    Wang, S.S.3    Phillips, M.4    Cascio, D.5    Eisenberg, D.6
  • 21
    • 34447511082 scopus 로고    scopus 로고
    • Tryptophan 32 potentiates aggregation and cytotoxicity of a copper/zinc superoxide dismutase mutant associated with familial amyotrophic lateral sclerosis
    • Taylor, D. M., Gibbs, B. F., Kabashi, E., Minotti, S., Durham, H. D., and Agar, J. N. (2007) Tryptophan 32 potentiates aggregation and cytotoxicity of a copper/zinc superoxide dismutase mutant associated with familial amyotrophic lateral sclerosis J. Biol. Chem. 282, 16329-16335
    • (2007) J. Biol. Chem. , vol.282 , pp. 16329-16335
    • Taylor, D.M.1    Gibbs, B.F.2    Kabashi, E.3    Minotti, S.4    Durham, H.D.5    Agar, J.N.6
  • 23
    • 84872381367 scopus 로고    scopus 로고
    • Structural switching of Cu,Zn-superoxide dismutases at loop VI: Insights from the crystal structure of beta-mercaptoethanol modified enzyme
    • Ihara, K., Fujiwara, N., Yamaguchi, Y., Torigoe, H., Wakatsuki, S., Taniguchi, N., and Suzuki, K. (2012) Structural switching of Cu,Zn-superoxide dismutases at loop VI: Insights from the crystal structure of beta-mercaptoethanol modified enzyme Biosci. Rep. 32, 539-548
    • (2012) Biosci. Rep. , vol.32 , pp. 539-548
    • Ihara, K.1    Fujiwara, N.2    Yamaguchi, Y.3    Torigoe, H.4    Wakatsuki, S.5    Taniguchi, N.6    Suzuki, K.7
  • 24
    • 0023655050 scopus 로고
    • Proteins damaged by oxygen radicals are rapidly degraded in extracts of red blood cells
    • Davies, K. J. and Goldberg, A. L. (1987) Proteins damaged by oxygen radicals are rapidly degraded in extracts of red blood cells J. Biol. Chem. 262, 8227-8234
    • (1987) J. Biol. Chem. , vol.262 , pp. 8227-8234
    • Davies, K.J.1    Goldberg, A.L.2
  • 25
    • 0023655258 scopus 로고
    • Oxygen radicals stimulate intracellular proteolysis and lipid peroxidation by independent mechanisms in erythrocytes
    • Davies, K. J. and Goldberg, A. L. (1987) Oxygen radicals stimulate intracellular proteolysis and lipid peroxidation by independent mechanisms in erythrocytes J. Biol. Chem. 262, 8220-8226
    • (1987) J. Biol. Chem. , vol.262 , pp. 8220-8226
    • Davies, K.J.1    Goldberg, A.L.2
  • 26
    • 0030811118 scopus 로고    scopus 로고
    • Do posttranslational modifications of CuZnSOD lead to sporadic amyotrophic lateral sclerosis?
    • Bredesen, D. E., Ellerby, L. M., Hart, P. J., Wiedau-Pazos, M., and Valentine, J. S. (1997) Do posttranslational modifications of CuZnSOD lead to sporadic amyotrophic lateral sclerosis? Ann. Neurol. 42, 135-137
    • (1997) Ann. Neurol. , vol.42 , pp. 135-137
    • Bredesen, D.E.1    Ellerby, L.M.2    Hart, P.J.3    Wiedau-Pazos, M.4    Valentine, J.S.5
  • 27
    • 37849007550 scopus 로고    scopus 로고
    • Oxidized/misfolded superoxide dismutase-1: The cause of all amyotrophic lateral sclerosis?
    • Kabashi, E., Valdmanis, P. N., Dion, P., and Rouleau, G. A. (2007) Oxidized/misfolded superoxide dismutase-1: the cause of all amyotrophic lateral sclerosis? Ann. Neurol. 62, 553-559
    • (2007) Ann. Neurol. , vol.62 , pp. 553-559
    • Kabashi, E.1    Valdmanis, P.N.2    Dion, P.3    Rouleau, G.A.4
  • 28
    • 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., Crow, J. P., Lepock, J. R., Kondejewski, L. H., Cashman, N. R., 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
    • (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    Chakrabartty, A.6
  • 31
    • 15744398884 scopus 로고    scopus 로고
    • Oxidative modifications and aggregation of Cu,Zn-superoxide dismutase associated with Alzheimer and Parkinson diseases
    • Choi, J., Rees, H. D., Weintraub, S. T., Levey, A. I., Chin, L. S., and Li, L. (2005) Oxidative modifications and aggregation of Cu,Zn-superoxide dismutase associated with Alzheimer and Parkinson diseases J. Biol. Chem. 280, 11648-11655
    • (2005) J. Biol. Chem. , vol.280 , pp. 11648-11655
    • Choi, J.1    Rees, H.D.2    Weintraub, S.T.3    Levey, A.I.4    Chin, L.S.5    Li, L.6
  • 32
    • 71449104857 scopus 로고    scopus 로고
    • A common property of amyotrophic lateral sclerosis-associated variants: Destabilization of the copper/zinc superoxide dismutase electrostatic loop
    • Molnar, K. S., Karabacak, N. M., Johnson, J. L., Wang, Q., Tiwari, A., Hayward, L. J., Coales, S. J., Hamuro, Y., and Agar, J. N. (2009) A common property of amyotrophic lateral sclerosis-associated variants: destabilization of the copper/zinc superoxide dismutase electrostatic loop J. Biol. Chem. 284, 30965-30973
    • (2009) J. Biol. Chem. , vol.284 , pp. 30965-30973
    • Molnar, K.S.1    Karabacak, N.M.2    Johnson, J.L.3    Wang, Q.4    Tiwari, A.5    Hayward, L.J.6    Coales, S.J.7    Hamuro, Y.8    Agar, J.N.9
  • 33
    • 33751536847 scopus 로고    scopus 로고
    • The coupling between disulphide status, metallation and dimer interface strength in Cu/Zn superoxide dismutase
    • Hornberg, A., Logan, D. T., Marklund, S. L., and Oliveberg, M. (2007) The coupling between disulphide status, metallation and dimer interface strength in Cu/Zn superoxide dismutase J. Mol. Biol. 365, 333-342
    • (2007) J. Mol. Biol. , vol.365 , pp. 333-342
    • Hornberg, A.1    Logan, D.T.2    Marklund, S.L.3    Oliveberg, M.4


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