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Volumn 1804, Issue 2, 2010, Pages 245-262

The structural biochemistry of the superoxide dismutases

Author keywords

Amyotrophic lateral sclerosis; Lou Gehrig's disease; Protein crystallography; Reactive oxygen species; Superoxide dismutase

Indexed keywords

COPPER ZINC SUPEROXIDE DISMUTASE; DIMER; DISULFIDE; HYDROGEN; IRON SUPEROXIDE DISMUTASE; LIGAND; MANGANESE SUPEROXIDE DISMUTASE; METAL; NICKEL SUPEROXIDE DISMUTASE; PHOSPHATE; SUPEROXIDE DISMUTASE; UNCLASSIFIED DRUG;

EID: 74649085703     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2009.11.004     Document Type: Review
Times cited : (427)

References (289)
  • 1
    • 0014691242 scopus 로고
    • Superoxide dismutase. An enzymic function for erythrocuprein (hemocuprein)
    • McCord J.M., and Fridovich I. Superoxide dismutase. An enzymic function for erythrocuprein (hemocuprein). J. Biol. Chem. 244 (1969) 6049-6055
    • (1969) J. Biol. Chem. , vol.244 , pp. 6049-6055
    • McCord, J.M.1    Fridovich, I.2
  • 2
    • 0030806863 scopus 로고    scopus 로고
    • Superoxide anion radical (O2-.), superoxide dismutases, and related matters
    • Fridovich I. Superoxide anion radical (O2-.), superoxide dismutases, and related matters. J. Biol. Chem. 272 (1997) 18515-18517
    • (1997) J. Biol. Chem. , vol.272 , pp. 18515-18517
    • Fridovich, I.1
  • 5
    • 0015596284 scopus 로고
    • Biological defense mechanisms. The production by leukocytes of superoxide, a potential bactericidal agent
    • Babior B.M., Kipnes R.S., and Curnutte J.T. Biological defense mechanisms. The production by leukocytes of superoxide, a potential bactericidal agent. J. Clin. Invest. 52 (1973) 741-744
    • (1973) J. Clin. Invest. , vol.52 , pp. 741-744
    • Babior, B.M.1    Kipnes, R.S.2    Curnutte, J.T.3
  • 6
    • 0018095849 scopus 로고
    • Increased superoxide anion production by immunologically activated and chemically elicited macrophages
    • Johnston Jr. R.B., Godzik C.A., and Cohn Z.A. Increased superoxide anion production by immunologically activated and chemically elicited macrophages. J. Exp. Med. 148 (1978) 115-127
    • (1978) J. Exp. Med. , vol.148 , pp. 115-127
    • Johnston Jr., R.B.1    Godzik, C.A.2    Cohn, Z.A.3
  • 8
    • 0000106023 scopus 로고
    • How innocuous is superoxide? Reply to comments
    • Sawyer D.T.V., and Valentine J.S. How innocuous is superoxide? Reply to comments. Acc. Chem. Res. 15 (1982) 200
    • (1982) Acc. Chem. Res. , vol.15 , pp. 200
    • Sawyer, D.T.V.1    Valentine, J.S.2
  • 9
    • 0015056379 scopus 로고
    • An enzyme-based theory of obligate anaerobiosis: the physiological function of superoxide dismutase
    • McCord J.M., Keele Jr. B.B., and Fridovich I. An enzyme-based theory of obligate anaerobiosis: the physiological function of superoxide dismutase. Proc. Natl. Acad. Sci. U. S. A. 68 (1971) 1024-1027
    • (1971) Proc. Natl. Acad. Sci. U. S. A. , vol.68 , pp. 1024-1027
    • McCord, J.M.1    Keele Jr., B.B.2    Fridovich, I.3
  • 10
    • 0000146818 scopus 로고
    • Superoxide and superoxide-dependent formation of hyrdoxyl radicals are important in oxygen-toxicity
    • Halliwell B., and J.M.C. Superoxide and superoxide-dependent formation of hyrdoxyl radicals are important in oxygen-toxicity. Trends Biochem. Sci. 7 (1982) 270-272
    • (1982) Trends Biochem. Sci. , vol.7 , pp. 270-272
    • Halliwell, B.1
  • 11
    • 0022683672 scopus 로고
    • Isolation of superoxide dismutase mutants in Escherichia coli: is superoxide dismutase necessary for aerobic life?
    • Carlioz A., and Touati D. Isolation of superoxide dismutase mutants in Escherichia coli: is superoxide dismutase necessary for aerobic life?. EMBO J. 5 (1986) 623-630
    • (1986) EMBO J. , vol.5 , pp. 623-630
    • Carlioz, A.1    Touati, D.2
  • 12
    • 0016170149 scopus 로고
    • Free radicals and inflammation: protection of synovial fluid by superoxide dismutase
    • McCord J.M. Free radicals and inflammation: protection of synovial fluid by superoxide dismutase. Science 185 (1974) 529-531
    • (1974) Science , vol.185 , pp. 529-531
    • McCord, J.M.1
  • 13
    • 0016751633 scopus 로고
    • Free radicals and inflammation. Protection of phagocytosine leukocytes by superoxide dismutase
    • Salin M.L., and McCord J.M. Free radicals and inflammation. Protection of phagocytosine leukocytes by superoxide dismutase. J. Clin. Invest. 56 (1975) 1319-1323
    • (1975) J. Clin. Invest. , vol.56 , pp. 1319-1323
    • Salin, M.L.1    McCord, J.M.2
  • 14
    • 0018902308 scopus 로고
    • Free radicals and inflammation: superoxide-dependent activation of a neutrophil chemotactic factor in plasma
    • Petrone W.F., English D.K., Wong K., and McCord J.M. Free radicals and inflammation: superoxide-dependent activation of a neutrophil chemotactic factor in plasma. Proc. Natl. Acad. Sci. U. S. A. 77 (1980) 1159-1163
    • (1980) Proc. Natl. Acad. Sci. U. S. A. , vol.77 , pp. 1159-1163
    • Petrone, W.F.1    English, D.K.2    Wong, K.3    McCord, J.M.4
  • 15
    • 0016826587 scopus 로고
    • Biogenesis of chemotactic molecules by the arachidonate lipoxygenase system of platelets
    • Turner S.R., Tainer J.A., and Lynn W.S. Biogenesis of chemotactic molecules by the arachidonate lipoxygenase system of platelets. Nature 257 (1975) 680-681
    • (1975) Nature , vol.257 , pp. 680-681
    • Turner, S.R.1    Tainer, J.A.2    Lynn, W.S.3
  • 16
    • 0023905646 scopus 로고
    • Toxic DNA damage by hydrogen peroxide through the Fenton reaction in vivo and in vitro
    • Imlay J.A., Chin S.M., and Linn S. Toxic DNA damage by hydrogen peroxide through the Fenton reaction in vivo and in vitro. Science 240 (1988) 640-642
    • (1988) Science , vol.240 , pp. 640-642
    • Imlay, J.A.1    Chin, S.M.2    Linn, S.3
  • 17
    • 0023886170 scopus 로고
    • DNA damage and oxygen radical toxicity
    • Imlay J.A., and Linn S. DNA damage and oxygen radical toxicity. Science 240 (1988) 1302-1309
    • (1988) Science , vol.240 , pp. 1302-1309
    • Imlay, J.A.1    Linn, S.2
  • 18
    • 34247157961 scopus 로고    scopus 로고
    • Developing master keys to brain pathology, cancer and aging from the structural biology of proteins controlling reactive oxygen species and DNA repair
    • Perry J.J., Fan L., and Tainer J.A. Developing master keys to brain pathology, cancer and aging from the structural biology of proteins controlling reactive oxygen species and DNA repair. Neuroscience 145 (2007) 1280-1299
    • (2007) Neuroscience , vol.145 , pp. 1280-1299
    • Perry, J.J.1    Fan, L.2    Tainer, J.A.3
  • 19
    • 0026754574 scopus 로고
    • Reactive oxygen species and the central nervous system
    • Halliwell B. Reactive oxygen species and the central nervous system. J. Neurochem. 59 (1992) 1609-1623
    • (1992) J. Neurochem. , vol.59 , pp. 1609-1623
    • Halliwell, B.1
  • 20
    • 0030133352 scopus 로고    scopus 로고
    • Blood radicals: reactive nitrogen species, reactive oxygen species, transition metal ions, and the vascular system
    • Darley-Usmar V., and Halliwell B. Blood radicals: reactive nitrogen species, reactive oxygen species, transition metal ions, and the vascular system. Pharm. Res. 13 (1996) 649-662
    • (1996) Pharm. Res. , vol.13 , pp. 649-662
    • Darley-Usmar, V.1    Halliwell, B.2
  • 21
    • 0030049032 scopus 로고    scopus 로고
    • Damage to DNA by reactive oxygen and nitrogen species: role in inflammatory disease and progression to cancer
    • Wiseman H., and Halliwell B. Damage to DNA by reactive oxygen and nitrogen species: role in inflammatory disease and progression to cancer. Biochem. J. 313 Pt. 1 (1996) 17-29
    • (1996) Biochem. J. , vol.313 , Issue.PART 1 , pp. 17-29
    • Wiseman, H.1    Halliwell, B.2
  • 22
    • 0031010333 scopus 로고    scopus 로고
    • Reactive oxygen-mediated protein oxidation in aging and disease
    • Stadtman E.R., and Berlett B.S. Reactive oxygen-mediated protein oxidation in aging and disease. Chem. Res. Toxicol. 10 (1997) 485-494
    • (1997) Chem. Res. Toxicol. , vol.10 , pp. 485-494
    • Stadtman, E.R.1    Berlett, B.S.2
  • 23
    • 0024780087 scopus 로고
    • Free radicals, reactive oxygen species and human disease: a critical evaluation with special reference to atherosclerosis
    • Halliwell B. Free radicals, reactive oxygen species and human disease: a critical evaluation with special reference to atherosclerosis. Br. J. Exp. Pathol. 70 (1989) 737-757
    • (1989) Br. J. Exp. Pathol. , vol.70 , pp. 737-757
    • Halliwell, B.1
  • 24
    • 0018749490 scopus 로고
    • Role of superoxide dismutase in cancer: a review
    • Oberley L.W., and Buettner G.R. Role of superoxide dismutase in cancer: a review. Cancer Res. 39 (1979) 1141-1149
    • (1979) Cancer Res. , vol.39 , pp. 1141-1149
    • Oberley, L.W.1    Buettner, G.R.2
  • 25
    • 0019440515 scopus 로고
    • Superoxide radicals in feline intestinal ischemia
    • Granger D.N., Rutili G., and McCord J.M. Superoxide radicals in feline intestinal ischemia. Gastroenterology 81 (1981) 22-29
    • (1981) Gastroenterology , vol.81 , pp. 22-29
    • Granger, D.N.1    Rutili, G.2    McCord, J.M.3
  • 27
    • 0842331263 scopus 로고
    • Superoxide dismutase: correlation with life-span and specific metabolic rate in primate species
    • Tolmasoff J.M., Ono T., and Cutler R.G. Superoxide dismutase: correlation with life-span and specific metabolic rate in primate species. Proc. Natl. Acad. Sci. U. S. A. 77 (1980) 2777-2781
    • (1980) Proc. Natl. Acad. Sci. U. S. A. , vol.77 , pp. 2777-2781
    • Tolmasoff, J.M.1    Ono, T.2    Cutler, R.G.3
  • 28
    • 0028220114 scopus 로고
    • Extension of life-span by overexpression of superoxide dismutase and catalase in Drosophila melanogaster
    • Orr W.C., and Sohal R.S. Extension of life-span by overexpression of superoxide dismutase and catalase in Drosophila melanogaster. Science 263 (1994) 1128-1130
    • (1994) Science , vol.263 , pp. 1128-1130
    • Orr, W.C.1    Sohal, R.S.2
  • 29
    • 0023007009 scopus 로고
    • Superoxide dismutase and catalase reduce infarct size in a porcine myocardial occlusion-reperfusion model
    • Naslund U., Haggmark S., Johansson G., Marklund S.L., Reiz S., and Oberg A. Superoxide dismutase and catalase reduce infarct size in a porcine myocardial occlusion-reperfusion model. J. Mol. Cell Cardiol. 18 (1986) 1077-1084
    • (1986) J. Mol. Cell Cardiol. , vol.18 , pp. 1077-1084
    • Naslund, U.1    Haggmark, S.2    Johansson, G.3    Marklund, S.L.4    Reiz, S.5    Oberg, A.6
  • 30
    • 70450224092 scopus 로고    scopus 로고
    • Antioxidant treatment with tempol and apocynin prevents endothelial dysfunction and development of renovascular hypertension
    • [Electronic publication ahead of print 2009 Sep 24]
    • Costa C.A., Amaral T.A., Carvalho L.C., Ognibene D.T., da Silva A.F., Moss M.B., Valenca S.S., de Moura R.S., and Resende A.C. Antioxidant treatment with tempol and apocynin prevents endothelial dysfunction and development of renovascular hypertension. Am. J. Hypertens. 22 12 (2009) 1242-1249 [Electronic publication ahead of print 2009 Sep 24]
    • (2009) Am. J. Hypertens. , vol.22 , Issue.12 , pp. 1242-1249
    • Costa, C.A.1    Amaral, T.A.2    Carvalho, L.C.3    Ognibene, D.T.4    da Silva, A.F.5    Moss, M.B.6    Valenca, S.S.7    de Moura, R.S.8    Resende, A.C.9
  • 31
    • 63049112375 scopus 로고    scopus 로고
    • Antioxidant therapeutic advances in COPD
    • Rahman I. Antioxidant therapeutic advances in COPD. Ther. Adv. Respir. Dis. 2 (2008) 351-374
    • (2008) Ther. Adv. Respir. Dis. , vol.2 , pp. 351-374
    • Rahman, I.1
  • 33
    • 67749142090 scopus 로고    scopus 로고
    • Inhibition of lipid infusion-induced skeletal muscle insulin resistance by cotreatment with tempol and glutathione in mice
    • Kim B.S., Cha H.N., Kim Y.W., Kim J.Y., Dan J.M., and Park S.Y. Inhibition of lipid infusion-induced skeletal muscle insulin resistance by cotreatment with tempol and glutathione in mice. J. Pharmacol. Sci. 110 (2009) 370-380
    • (2009) J. Pharmacol. Sci. , vol.110 , pp. 370-380
    • Kim, B.S.1    Cha, H.N.2    Kim, Y.W.3    Kim, J.Y.4    Dan, J.M.5    Park, S.Y.6
  • 34
    • 65649084453 scopus 로고    scopus 로고
    • Protective effects of a superoxide dismutase/catalase mimetic compound against paraquat pneumotoxicity in rat lung
    • Shopova V.L., Dancheva V.Y., Salovsky P.T., and Stoyanova A.M. Protective effects of a superoxide dismutase/catalase mimetic compound against paraquat pneumotoxicity in rat lung. Respirology 14 (2009) 504-510
    • (2009) Respirology , vol.14 , pp. 504-510
    • Shopova, V.L.1    Dancheva, V.Y.2    Salovsky, P.T.3    Stoyanova, A.M.4
  • 35
    • 70449579447 scopus 로고    scopus 로고
    • Superoxide dismutase analog (Tempol: 4-hydroxy-2, 2, 6, 6-tetramethylpiperidine 1-oxyl) treatment restores erectile function in diabetes-induced impotence
    • [Electronic publication ahead of print 25 June 2009]
    • Kawakami T., Urakami S., Hirata H., Tanaka Y., Nakajima K., Enokida H., Shiina H., Ogishima T., Tokizane T., Kawamoto K., Miura K., Ishii N., and Dahiya R. Superoxide dismutase analog (Tempol: 4-hydroxy-2, 2, 6, 6-tetramethylpiperidine 1-oxyl) treatment restores erectile function in diabetes-induced impotence. Int. J. Impot. Res. 21 (2009) 348-355 [Electronic publication ahead of print 25 June 2009]
    • (2009) Int. J. Impot. Res. , vol.21 , pp. 348-355
    • Kawakami, T.1    Urakami, S.2    Hirata, H.3    Tanaka, Y.4    Nakajima, K.5    Enokida, H.6    Shiina, H.7    Ogishima, T.8    Tokizane, T.9    Kawamoto, K.10    Miura, K.11    Ishii, N.12    Dahiya, R.13
  • 36
    • 53449089230 scopus 로고    scopus 로고
    • Antioxidant SOD mimetic prevents NADPH oxidase-induced oxidative stress and renal damage in the early stage of experimental diabetes and hypertension
    • Peixoto E.B., Pessoa B.S., Biswas S.K., and Lopes de Faria J.B. Antioxidant SOD mimetic prevents NADPH oxidase-induced oxidative stress and renal damage in the early stage of experimental diabetes and hypertension. Am. J. Nephrol. 29 (2009) 309-318
    • (2009) Am. J. Nephrol. , vol.29 , pp. 309-318
    • Peixoto, E.B.1    Pessoa, B.S.2    Biswas, S.K.3    Lopes de Faria, J.B.4
  • 37
    • 58249134576 scopus 로고    scopus 로고
    • TEMPOL, a membrane-permeable radical scavenger, attenuates gastric mucosal damage induced by ischemia/reperfusion: a key role for superoxide anion
    • Abdallah D.M., El-Abhar H.S., and Abdel-Aziz D.H. TEMPOL, a membrane-permeable radical scavenger, attenuates gastric mucosal damage induced by ischemia/reperfusion: a key role for superoxide anion. Eur. J. Pharmacol. 603 (2009) 93-97
    • (2009) Eur. J. Pharmacol. , vol.603 , pp. 93-97
    • Abdallah, D.M.1    El-Abhar, H.S.2    Abdel-Aziz, D.H.3
  • 39
    • 0016680344 scopus 로고
    • W, Problems concerning the biochemical action of superoxide dismutase (erthrocuperin)
    • Paschen W.U. W, Problems concerning the biochemical action of superoxide dismutase (erthrocuperin). Hoppe Seylers Z. Physiol. Chem. 356 (1975) 727-737
    • (1975) Hoppe Seylers Z. Physiol. Chem. , vol.356 , pp. 727-737
    • Paschen, W.U.1
  • 40
    • 0023028704 scopus 로고
    • Phosphate inhibition of the copper-and zinc-containing superoxide dismutase: a reexamination
    • Beyer Jr. W.F., Wang Y., and Fridovich I. Phosphate inhibition of the copper-and zinc-containing superoxide dismutase: a reexamination. Biochemistry 25 (1986) 6084-6088
    • (1986) Biochemistry , vol.25 , pp. 6084-6088
    • Beyer Jr., W.F.1    Wang, Y.2    Fridovich, I.3
  • 41
    • 0021081808 scopus 로고
    • Structure and mechanism of copper, zinc superoxide dismutase
    • Tainer J.A., Getzoff E.D., Richardson J.S., and Richardson D.C. Structure and mechanism of copper, zinc superoxide dismutase. Nature 306 (1983) 284-287
    • (1983) Nature , vol.306 , pp. 284-287
    • Tainer, J.A.1    Getzoff, E.D.2    Richardson, J.S.3    Richardson, D.C.4
  • 43
    • 0021369433 scopus 로고
    • Phosphate is an inhibitor of copper-zinc superoxide dismutase
    • Mota de Freitas D., and Valentine J.S. Phosphate is an inhibitor of copper-zinc superoxide dismutase. Biochemistry 23 (1984) 2079-2082
    • (1984) Biochemistry , vol.23 , pp. 2079-2082
    • Mota de Freitas, D.1    Valentine, J.S.2
  • 49
    • 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 Dokholyan N.V. Dynamical roles of metal ions and the disulfide bond in Cu, Zn superoxide dismutase folding and aggregation. Proc. Natl. Acad. Sci. U. S. A. 105 (2008) 19696-19701
    • (2008) Proc. Natl. Acad. Sci. U. S. A. , vol.105 , pp. 19696-19701
    • Ding, F.1    Dokholyan, N.V.2
  • 51
    • 62149129690 scopus 로고    scopus 로고
    • Destabilizing protein polymorphisms in the genetic background direct phenotypic expression of mutant SOD1 toxicity
    • Gidalevitz T., Krupinski T., Garcia S., and Morimoto R.I. Destabilizing protein polymorphisms in the genetic background direct phenotypic expression of mutant SOD1 toxicity. PLoS Genet. 5 (2009) e1000399
    • (2009) PLoS Genet. , vol.5
    • Gidalevitz, T.1    Krupinski, T.2    Garcia, S.3    Morimoto, R.I.4
  • 52
    • 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. The coupling between disulphide status, metallation and dimer interface strength in Cu/Zn superoxide dismutase. J. Mol. Biol. 365 (2007) 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
  • 54
    • 22244489417 scopus 로고    scopus 로고
    • Systematically perturbed folding patterns of amyotrophic lateral sclerosis (ALS)-associated SOD1 mutants
    • Lindberg M.J., Bystrom R., Boknas N., Andersen P.M., and Oliveberg M. Systematically perturbed folding patterns of amyotrophic lateral sclerosis (ALS)-associated SOD1 mutants. Proc. Natl. Acad. Sci. U. S. A. 102 (2005) 9754-9759
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 9754-9759
    • Lindberg, M.J.1    Bystrom, R.2    Boknas, N.3    Andersen, P.M.4    Oliveberg, M.5
  • 55
    • 74649086999 scopus 로고    scopus 로고
    • SOD1-associated ALS: a promising system for elucidating the origin of protein-misfolding disease
    • Nordlund A., and Oliveberg M. SOD1-associated ALS: a promising system for elucidating the origin of protein-misfolding disease. HFSP J. 2 (2008) 354-364
    • (2008) HFSP J. , vol.2 , pp. 354-364
    • Nordlund, A.1    Oliveberg, M.2
  • 57
    • 57749208693 scopus 로고    scopus 로고
    • Unfolding and folding kinetics of amyotrophic lateral sclerosis-associated mutant Cu,Zn superoxide dismutases
    • Rumfeldt J.A., Lepock J.R., and Meiering E.M. Unfolding and folding kinetics of amyotrophic lateral sclerosis-associated mutant Cu,Zn superoxide dismutases. J. Mol. Biol. 385 (2009) 278-298
    • (2009) J. Mol. Biol. , vol.385 , pp. 278-298
    • Rumfeldt, J.A.1    Lepock, J.R.2    Meiering, E.M.3
  • 58
    • 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., Durazo A., Nersissian A.M., Whitelegge J.P., Faull K.F., and Valentine J.S. Local unfolding in a destabilized, pathogenic variant of superoxide dismutase 1 observed with H/D exchange and mass spectrometry. J. Biol. Chem. 281 (2006) 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    Valentine, J.S.6
  • 59
    • 58549114655 scopus 로고    scopus 로고
    • Superoxide dismutase from the eukaryotic thermophile Alvinella pompejana: structures, stability, mechanism, and insights into amyotrophic lateral sclerosis
    • Shin D.S., Didonato M., Barondeau D.P., Hura G.L., Hitomi C., Berglund J.A., Getzoff E.D., Cary S.C., and Tainer J.A. Superoxide dismutase from the eukaryotic thermophile Alvinella pompejana: structures, stability, mechanism, and insights into amyotrophic lateral sclerosis. J. Mol. Biol. 385 (2009) 1534-1555
    • (2009) J. Mol. Biol. , vol.385 , pp. 1534-1555
    • Shin, D.S.1    Didonato, M.2    Barondeau, D.P.3    Hura, G.L.4    Hitomi, C.5    Berglund, J.A.6    Getzoff, E.D.7    Cary, S.C.8    Tainer, J.A.9
  • 60
    • 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., Yong C.W., Smith W., and Hasnain S.S. Molecular dynamics using atomic-resolution structure reveal structural fluctuations that may lead to polymerization of human Cu-Zn superoxide dismutase. Proc. Natl. Acad. Sci. U. S. A. 104 (2007) 10040-10044
    • (2007) Proc. Natl. Acad. Sci. U. S. A. , vol.104 , pp. 10040-10044
    • Strange, R.W.1    Yong, C.W.2    Smith, W.3    Hasnain, S.S.4
  • 61
    • 70350435485 scopus 로고    scopus 로고
    • Metal deficiency increases aberrant hydrophobicity of mutant superoxide dismutases that cause amyotrophic lateral sclerosis
    • [Electronic publication ahead of print 2009 Aug 3]
    • Tiwari A., Liba A., Sohn S.H., Seetharaman S.V., Bilsel O., Matthews C.R., Hart P.J., Valentine J.S., and Hayward L.J. Metal deficiency increases aberrant hydrophobicity of mutant superoxide dismutases that cause amyotrophic lateral sclerosis. J. Biol. Chem. 284 40 (2009) 27746-27758 [Electronic publication ahead of print 2009 Aug 3]
    • (2009) J. Biol. Chem. , vol.284 , Issue.40 , pp. 27746-27758
    • Tiwari, A.1    Liba, A.2    Sohn, S.H.3    Seetharaman, S.V.4    Bilsel, O.5    Matthews, C.R.6    Hart, P.J.7    Valentine, J.S.8    Hayward, L.J.9
  • 62
    • 59249098430 scopus 로고    scopus 로고
    • An ALS-linked mutant SOD1 produces a locomotor defect associated with aggregation and synaptic dysfunction when expressed in neurons of Caenorhabditis elegans
    • Wang J., Farr G.W., Hall D.H., Li F., Furtak K., Dreier L., and Horwich A.L. An ALS-linked mutant SOD1 produces a locomotor defect associated with aggregation and synaptic dysfunction when expressed in neurons of Caenorhabditis elegans. PLoS Genet. 5 (2009) e1000350
    • (2009) PLoS Genet. , vol.5
    • Wang, J.1    Farr, G.W.2    Hall, D.H.3    Li, F.4    Furtak, K.5    Dreier, L.6    Horwich, A.L.7
  • 63
    • 48349090111 scopus 로고    scopus 로고
    • Protein aggregation and protein instability govern familial amyotrophic lateral sclerosis patient survival
    • Wang Q., Johnson J.L., Agar N.Y., and Agar J.N. Protein aggregation and protein instability govern familial amyotrophic lateral sclerosis patient survival. PLoS Biol. 6 (2008) e170
    • (2008) PLoS Biol. , vol.6
    • Wang, Q.1    Johnson, J.L.2    Agar, N.Y.3    Agar, J.N.4
  • 66
    • 0042632880 scopus 로고    scopus 로고
    • Genetic epidemiology of amyotrophic lateral sclerosis
    • Majoor-Krakauer D., Willems P.J., and Hofman A. Genetic epidemiology of amyotrophic lateral sclerosis. Clin. Genet. 63 (2003) 83-101
    • (2003) Clin. Genet. , vol.63 , pp. 83-101
    • Majoor-Krakauer, D.1    Willems, P.J.2    Hofman, A.3
  • 67
    • 31544466502 scopus 로고    scopus 로고
    • Amyotrophic lateral sclerosis associated with mutations in the CuZn superoxide dismutase gene
    • Andersen P.M. Amyotrophic lateral sclerosis associated with mutations in the CuZn superoxide dismutase gene. Curr. Neurol. Neurosci. Rep. 6 (2006) 37-46
    • (2006) Curr. Neurol. Neurosci. Rep. , vol.6 , pp. 37-46
    • Andersen, P.M.1
  • 68
    • 0026633193 scopus 로고
    • A comparison of evolutionary rates of the two major kinds of superoxide dismutase
    • Smith M.W., and Doolittle R.F. A comparison of evolutionary rates of the two major kinds of superoxide dismutase. J. Mol. Evol. 34 (1992) 175-184
    • (1992) J. Mol. Evol. , vol.34 , pp. 175-184
    • Smith, M.W.1    Doolittle, R.F.2
  • 69
    • 0001596728 scopus 로고
    • Haemocuprein and hepatocuprein, copper-protein compounds of blood and liver in mammals
    • Mann T., and Keilin D. Haemocuprein and hepatocuprein, copper-protein compounds of blood and liver in mammals. Proc. Roy. Soc. Ser. B-Biol. Sci. 126 (1938) 303-315
    • (1938) Proc. Roy. Soc. Ser. B-Biol. Sci. , vol.126 , pp. 303-315
    • Mann, T.1    Keilin, D.2
  • 70
    • 70449251565 scopus 로고
    • Some chemical and physical properties of erythrocuprein
    • Kimmel J.R., Markowitz H., and Brown D.M. Some chemical and physical properties of erythrocuprein. J. Biol. Chem. 234 (1959) 46-50
    • (1959) J. Biol. Chem. , vol.234 , pp. 46-50
    • Kimmel, J.R.1    Markowitz, H.2    Brown, D.M.3
  • 71
    • 0012795202 scopus 로고
    • Studies on copper metabolism. XXVII. The isolation and properties of an erythrocyte cuproprotein (erythrocuprein)
    • Markowitz H., Cartwright G.E., and Wintrobe M.M. Studies on copper metabolism. XXVII. The isolation and properties of an erythrocyte cuproprotein (erythrocuprein). J. Biol. Chem. 234 (1959) 40-45
    • (1959) J. Biol. Chem. , vol.234 , pp. 40-45
    • Markowitz, H.1    Cartwright, G.E.2    Wintrobe, M.M.3
  • 72
    • 28244439742 scopus 로고
    • A copper-containing protein isolated from brain
    • Porter H., Folch J., and Cerebrocuprein I. A copper-containing protein isolated from brain. J. Neurochem. 1 (1957) 260-271
    • (1957) J. Neurochem. , vol.1 , pp. 260-271
    • Porter, H.1    Folch, J.2    Cerebrocuprein, I.3
  • 73
    • 0020374498 scopus 로고
    • Determination and analysis of the 2 A-structure of copper, zinc superoxide dismutase
    • Tainer J.A., Getzoff E.D., Beem K.M., Richardson J.S., and Richardson D.C. Determination and analysis of the 2 A-structure of copper, zinc superoxide dismutase. J. Mol. Biol. 160 (1982) 181-217
    • (1982) J. Mol. Biol. , vol.160 , pp. 181-217
    • Tainer, J.A.1    Getzoff, E.D.2    Beem, K.M.3    Richardson, J.S.4    Richardson, D.C.5
  • 75
    • 0026711256 scopus 로고
    • Atomic structures of wild-type and thermostable mutant recombinant human Cu,Zn superoxide dismutase
    • Parge H.E., Hallewell R.A., and Tainer J.A. Atomic structures of wild-type and thermostable mutant recombinant human Cu,Zn superoxide dismutase. Proc. Natl. Acad. Sci. U. S. A. 89 (1992) 6109-6113
    • (1992) Proc. Natl. Acad. Sci. U. S. A. , vol.89 , pp. 6109-6113
    • Parge, H.E.1    Hallewell, R.A.2    Tainer, J.A.3
  • 83
    • 0036231449 scopus 로고    scopus 로고
    • The solution structure of reduced dimeric copper zinc superoxide dismutase. The structural effects of dimerization
    • Banci L., Bertini I., Cramaro F., Del Conte R., and Viezzoli M.S. The solution structure of reduced dimeric copper zinc superoxide dismutase. The structural effects of dimerization. Eur. J. Biochem. 269 (2002) 1905-1915
    • (2002) Eur. J. Biochem. , vol.269 , pp. 1905-1915
    • Banci, L.1    Bertini, I.2    Cramaro, F.3    Del Conte, R.4    Viezzoli, M.S.5
  • 84
    • 0017387723 scopus 로고
    • β-Sheet topology and the relatedness of proteins
    • Richardson J.S. β-Sheet topology and the relatedness of proteins. Nature 268 (1977) 495-500
    • (1977) Nature , vol.268 , pp. 495-500
    • Richardson, J.S.1
  • 85
    • 0024411652 scopus 로고
    • Evolution of CuZn superoxide dismutase and the Greek key beta-barrel structural motif
    • Getzoff E.D., Tainer J.A., Stempien M.M., Bell G.I., and Hallewell R.A. Evolution of CuZn superoxide dismutase and the Greek key beta-barrel structural motif. Proteins 5 (1989) 322-336
    • (1989) Proteins , vol.5 , pp. 322-336
    • Getzoff, E.D.1    Tainer, J.A.2    Stempien, M.M.3    Bell, G.I.4    Hallewell, R.A.5
  • 87
    • 0025861597 scopus 로고
    • Electrostatic orientation of the electron-transfer complex between plastocyanin and cytochrome c
    • Roberts V.A., Freeman H.C., Olson A.J., Tainer J.A., and Getzoff E.D. Electrostatic orientation of the electron-transfer complex between plastocyanin and cytochrome c. J. Biol. Chem. 266 (1991) 13431-13441
    • (1991) J. Biol. Chem. , vol.266 , pp. 13431-13441
    • Roberts, V.A.1    Freeman, H.C.2    Olson, A.J.3    Tainer, J.A.4    Getzoff, E.D.5
  • 88
    • 0042131831 scopus 로고    scopus 로고
    • Structure of fully reduced bovine copper zinc superoxide dismutase at 1.15 A
    • Hough M.A., and Hasnain S.S. Structure of fully reduced bovine copper zinc superoxide dismutase at 1.15 A. Structure 11 (2003) 937-946
    • (2003) Structure , vol.11 , pp. 937-946
    • Hough, M.A.1    Hasnain, S.S.2
  • 89
    • 32044475396 scopus 로고    scopus 로고
    • Variable metallation of human superoxide dismutase: atomic resolution crystal structures of Cu-Zn, Zn-Zn and As-isolated wild-type enzymes
    • Strange R.W., Antonyuk S.V., Hough M.A., Doucette P.A., Valentine J.S., and Hasnain S.S. Variable metallation of human superoxide dismutase: atomic resolution crystal structures of Cu-Zn, Zn-Zn and As-isolated wild-type enzymes. J. Mol. Biol. 356 (2006) 1152-1162
    • (2006) J. Mol. Biol. , vol.356 , pp. 1152-1162
    • Strange, R.W.1    Antonyuk, S.V.2    Hough, M.A.3    Doucette, P.A.4    Valentine, J.S.5    Hasnain, S.S.6
  • 90
    • 0028228085 scopus 로고
    • Conserved patterns in the Cu,Zn superoxide dismutase family
    • Bordo D., Djinovic K., and Bolognesi M. Conserved patterns in the Cu,Zn superoxide dismutase family. J. Mol. Biol. 238 (1994) 366-386
    • (1994) J. Mol. Biol. , vol.238 , pp. 366-386
    • Bordo, D.1    Djinovic, K.2    Bolognesi, M.3
  • 94
    • 0030929123 scopus 로고    scopus 로고
    • Computational, pulse-radiolytic, and structural investigations of lysine-136 and its role in the electrostatic triad of human Cu,Zn superoxide dismutase
    • Fisher C.L., Cabelli D.E., Hallewell R.A., Beroza P., Lo T.P., Getzoff E.D., and Tainer J.A. Computational, pulse-radiolytic, and structural investigations of lysine-136 and its role in the electrostatic triad of human Cu,Zn superoxide dismutase. Proteins 29 (1997) 103-112
    • (1997) Proteins , vol.29 , pp. 103-112
    • Fisher, C.L.1    Cabelli, D.E.2    Hallewell, R.A.3    Beroza, P.4    Lo, T.P.5    Getzoff, E.D.6    Tainer, J.A.7
  • 95
    • 0028300739 scopus 로고
    • The role of arginine 143 in the electrostatics and mechanism of Cu,Zn superoxide dismutase: computational and experimental evaluation by mutational analysis
    • Fisher C.L., Cabelli D.E., Tainer J.A., Hallewell R.A., and Getzoff E.D. The role of arginine 143 in the electrostatics and mechanism of Cu,Zn superoxide dismutase: computational and experimental evaluation by mutational analysis. Proteins 19 (1994) 24-34
    • (1994) Proteins , vol.19 , pp. 24-34
    • Fisher, C.L.1    Cabelli, D.E.2    Tainer, J.A.3    Hallewell, R.A.4    Getzoff, E.D.5
  • 96
    • 0025930452 scopus 로고
    • Probing the structural basis for enzyme-substrate recognition in Cu,Zn superoxide dismutase
    • Fisher C.L., Hallewell R.A., Roberts V.A., Tainer J.A., and Getzoff E.D. Probing the structural basis for enzyme-substrate recognition in Cu,Zn superoxide dismutase. Free Radic. Res. Commun. 12-13 Pt. 1 (1991) 287-296
    • (1991) Free Radic. Res. Commun. , vol.12-13 , Issue.PART 1 , pp. 287-296
    • Fisher, C.L.1    Hallewell, R.A.2    Roberts, V.A.3    Tainer, J.A.4    Getzoff, E.D.5
  • 98
    • 0024262417 scopus 로고
    • Probing enzyme-substrate recognition and catalytic mechanism in Cu,Zn superoxide dismutase
    • Tainer J.A., Hallewell R.A., Roberts V.A., Parge H.E., and Getzoff E.D. Probing enzyme-substrate recognition and catalytic mechanism in Cu,Zn superoxide dismutase. Basic Life Sci. 49 (1988) 635-640
    • (1988) Basic Life Sci. , vol.49 , pp. 635-640
    • Tainer, J.A.1    Hallewell, R.A.2    Roberts, V.A.3    Parge, H.E.4    Getzoff, E.D.5
  • 100
    • 0031875278 scopus 로고    scopus 로고
    • Crystallographic determination of reduced bovine superoxide dismutase at pH 5.0 and of anion binding to its active site
    • Ferraroni M., Rypniewski W.R., Bruni B., Orioli P., and Mangani S. Crystallographic determination of reduced bovine superoxide dismutase at pH 5.0 and of anion binding to its active site. J. Biol. Inorg. Chem. 3 (1998) 411-422
    • (1998) J. Biol. Inorg. Chem. , vol.3 , pp. 411-422
    • Ferraroni, M.1    Rypniewski, W.R.2    Bruni, B.3    Orioli, P.4    Mangani, S.5
  • 101
    • 33845927105 scopus 로고    scopus 로고
    • Mechanisms of electron transfer in catalysis by copper zinc superoxide dismutase
    • Smirnov V.V., and Roth J.P. Mechanisms of electron transfer in catalysis by copper zinc superoxide dismutase. J. Am. Chem. Soc. 128 (2006) 16424-16425
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 16424-16425
    • Smirnov, V.V.1    Roth, J.P.2
  • 102
    • 64049104165 scopus 로고    scopus 로고
    • The structure of human extracellular copper-zinc superoxide dismutase at 1.7 A resolution: insights into heparin and collagen binding
    • Antonyuk S.V., Strange R.W., Marklund S.L., and Hasnain S.S. The structure of human extracellular copper-zinc superoxide dismutase at 1.7 A resolution: insights into heparin and collagen binding. J. Mol. Biol. 388 (2009) 310-326
    • (2009) J. Mol. Biol. , vol.388 , pp. 310-326
    • Antonyuk, S.V.1    Strange, R.W.2    Marklund, S.L.3    Hasnain, S.S.4
  • 103
    • 0021745377 scopus 로고
    • Extracellular superoxide dismutase in human tissues and human cell lines
    • Marklund S.L. Extracellular superoxide dismutase in human tissues and human cell lines. J. Clin. Invest. 74 (1984) 1398-1403
    • (1984) J. Clin. Invest. , vol.74 , pp. 1398-1403
    • Marklund, S.L.1
  • 104
    • 0021878710 scopus 로고
    • Product of extracellular-superoxide dismutase catalysis
    • Marklund S.L. Product of extracellular-superoxide dismutase catalysis. FEBS Lett. 184 (1985) 237-239
    • (1985) FEBS Lett. , vol.184 , pp. 237-239
    • Marklund, S.L.1
  • 105
    • 0029078783 scopus 로고
    • Copper, zinc superoxide dismutase in Escherichia coli: periplasmic localization
    • Benov L., Chang L.Y., Day B., and Fridovich I. Copper, zinc superoxide dismutase in Escherichia coli: periplasmic localization. Arch. Biochem. Biophys. 319 (1995) 508-511
    • (1995) Arch. Biochem. Biophys. , vol.319 , pp. 508-511
    • Benov, L.1    Chang, L.Y.2    Day, B.3    Fridovich, I.4
  • 106
    • 0029988780 scopus 로고    scopus 로고
    • Identification of sodC encoding periplasmic [Cu,Zn]-superoxide dismutase in Salmonella
    • Canvin J., Langford P.R., Wilks K.E., and Kroll J.S. Identification of sodC encoding periplasmic [Cu,Zn]-superoxide dismutase in Salmonella. FEMS. Microbiol. Lett. 136 (1996) 215-220
    • (1996) FEMS. Microbiol. Lett. , vol.136 , pp. 215-220
    • Canvin, J.1    Langford, P.R.2    Wilks, K.E.3    Kroll, J.S.4
  • 107
    • 0025885796 scopus 로고
    • Copper-zinc superoxide dismutase of Haemophilus influenzae and H. parainfluenzae
    • Kroll J.S., Langford P.R., and Loynds B.M. Copper-zinc superoxide dismutase of Haemophilus influenzae and H. parainfluenzae. J. Bacteriol. 173 (1991) 7449-7457
    • (1991) J. Bacteriol. , vol.173 , pp. 7449-7457
    • Kroll, J.S.1    Langford, P.R.2    Loynds, B.M.3
  • 108
    • 0028804901 scopus 로고
    • Bacterial [Cu,Zn]-superoxide dismutase: phylogenetically distinct from the eukaryotic enzyme, and not so rare after all!
    • Kroll J.S., Langford P.R., Wilks K.E., and Keil A.D. Bacterial [Cu,Zn]-superoxide dismutase: phylogenetically distinct from the eukaryotic enzyme, and not so rare after all!. Microbiology 141 Pt. 9 (1995) 2271-2279
    • (1995) Microbiology , vol.141 , Issue.PART 9 , pp. 2271-2279
    • Kroll, J.S.1    Langford, P.R.2    Wilks, K.E.3    Keil, A.D.4
  • 110
    • 0029806690 scopus 로고    scopus 로고
    • Cloning and molecular characterization of Cu,Zn superoxide dismutase from Actinobacillus pleuropneumoniae
    • Langford P.R., Loynds B.M., and Kroll J.S. Cloning and molecular characterization of Cu,Zn superoxide dismutase from Actinobacillus pleuropneumoniae. Infect. Immun. 64 (1996) 5035-5041
    • (1996) Infect. Immun. , vol.64 , pp. 5035-5041
    • Langford, P.R.1    Loynds, B.M.2    Kroll, J.S.3
  • 111
    • 0028212098 scopus 로고
    • Periplasmic location of Brucella abortus Cu/Zn superoxide dismutase
    • Stabel T.J., Sha Z., and Mayfield J.E. Periplasmic location of Brucella abortus Cu/Zn superoxide dismutase. Vet. Microbiol. 38 (1994) 307-314
    • (1994) Vet. Microbiol. , vol.38 , pp. 307-314
    • Stabel, T.J.1    Sha, Z.2    Mayfield, J.E.3
  • 113
    • 0026636510 scopus 로고
    • Construction of Cu-Zn superoxide dismutase deletion mutants of Brucella abortus: analysis of survival in vitro in epithelial and phagocytic cells and in vivo in mice
    • Tatum F.M., Detilleux P.G., Sacks J.M., and Halling S.M. Construction of Cu-Zn superoxide dismutase deletion mutants of Brucella abortus: analysis of survival in vitro in epithelial and phagocytic cells and in vivo in mice. Infect. Immun. 60 (1992) 2863-2869
    • (1992) Infect. Immun. , vol.60 , pp. 2863-2869
    • Tatum, F.M.1    Detilleux, P.G.2    Sacks, J.M.3    Halling, S.M.4
  • 115
    • 0348049821 scopus 로고    scopus 로고
    • Role of prokaryotic Cu,Zn superoxide dismutase in pathogenesis
    • Battistoni A. Role of prokaryotic Cu,Zn superoxide dismutase in pathogenesis. Biochem. Soc. Trans. 31 (2003) 1326-1329
    • (2003) Biochem. Soc. Trans. , vol.31 , pp. 1326-1329
    • Battistoni, A.1
  • 118
    • 0025357061 scopus 로고
    • Crystallographic characterization of a Cu,Zn superoxide dismutase from Photobacterium leiognathi
    • Redford S.M., McRee D.E., Getzoff E.D., Steinman H.M., and Tainer J.A. Crystallographic characterization of a Cu,Zn superoxide dismutase from Photobacterium leiognathi. J. Mol. Biol. 212 (1990) 449-451
    • (1990) J. Mol. Biol. , vol.212 , pp. 449-451
    • Redford, S.M.1    McRee, D.E.2    Getzoff, E.D.3    Steinman, H.M.4    Tainer, J.A.5
  • 120
    • 0034635343 scopus 로고    scopus 로고
    • Cu,Zn superoxide dismutase structure from a microbial pathogen establishes a class with a conserved dimer interface
    • Forest K.T., Langford P.R., Kroll J.S., and Getzoff E.D. Cu,Zn superoxide dismutase structure from a microbial pathogen establishes a class with a conserved dimer interface. J. Mol. Biol. 296 (2000) 145-153
    • (2000) J. Mol. Biol. , vol.296 , pp. 145-153
    • Forest, K.T.1    Langford, P.R.2    Kroll, J.S.3    Getzoff, E.D.4
  • 122
    • 0031555480 scopus 로고    scopus 로고
    • Unique structural features of the monomeric Cu,Zn superoxide dismutase from Escherichia coli, revealedZ by X-ray crystallography
    • Pesce A., Capasso C., Battistoni A., Folcarelli S., Rotilio G., Desideri A., and Bolognesi M. Unique structural features of the monomeric Cu,Zn superoxide dismutase from Escherichia coli, revealedZ by X-ray crystallography. J. Mol. Biol. 274 (1997) 408-420
    • (1997) J. Mol. Biol. , vol.274 , pp. 408-420
    • Pesce, A.1    Capasso, C.2    Battistoni, A.3    Folcarelli, S.4    Rotilio, G.5    Desideri, A.6    Bolognesi, M.7
  • 123
    • 0035516124 scopus 로고    scopus 로고
    • From Charcot to Lou Gehrig: deciphering selective motor neuron death in ALS
    • Cleveland D.W., and Rothstein J.D. From Charcot to Lou Gehrig: deciphering selective motor neuron death in ALS. Nat. Rev. Neurosci. 2 (2001) 806-819
    • (2001) Nat. Rev. Neurosci. , vol.2 , pp. 806-819
    • Cleveland, D.W.1    Rothstein, J.D.2
  • 124
    • 0000280462 scopus 로고
    • Deux cas d'atrophie musculaire progressive avec lesions de la substance grise et des faisceaux antero-lateraux de la moelle epiniere
    • Charcot J.M., and Joffory A. Deux cas d'atrophie musculaire progressive avec lesions de la substance grise et des faisceaux antero-lateraux de la moelle epiniere. Arch. Physiol. Neurol. Pathol. 2 (1869) 744-754
    • (1869) Arch. Physiol. Neurol. Pathol. , vol.2 , pp. 744-754
    • Charcot, J.M.1    Joffory, A.2
  • 125
    • 0029810307 scopus 로고    scopus 로고
    • Genetics of amyotrophic lateral sclerosis
    • Siddique T., and Deng H.X. Genetics of amyotrophic lateral sclerosis. Hum. Mol. Genet. 5 (1996) 1465-1470
    • (1996) Hum. Mol. Genet. , vol.5 , pp. 1465-1470
    • Siddique, T.1    Deng, H.X.2
  • 126
    • 0035237310 scopus 로고    scopus 로고
    • Protein folding and its links with human disease
    • Dobson C.M. Protein folding and its links with human disease. Biochem. Soc. Symp. (2001) 1-26
    • (2001) Biochem. Soc. Symp. , pp. 1-26
    • Dobson, C.M.1
  • 129
    • 34247505633 scopus 로고    scopus 로고
    • ALS: astrocytes move in as deadly neighbors
    • Julien J.P. ALS: astrocytes move in as deadly neighbors. Nat. Neurosci. 10 (2007) 535-537
    • (2007) Nat. Neurosci. , vol.10 , pp. 535-537
    • Julien, J.P.1
  • 130
    • 0038627546 scopus 로고    scopus 로고
    • The perplexing role of copper-zinc superoxide dismutase in amyotrophic lateral sclerosis (Lou Gehrig's disease)
    • Potter S.Z., and Valentine J.S. The perplexing role of copper-zinc superoxide dismutase in amyotrophic lateral sclerosis (Lou Gehrig's disease). J. Biol. Inorg. Chem. 8 (2003) 373-380
    • (2003) J. Biol. Inorg. Chem. , vol.8 , pp. 373-380
    • Potter, S.Z.1    Valentine, J.S.2
  • 132
    • 33846678063 scopus 로고    scopus 로고
    • How do ALS-associated mutations in superoxide dismutase 1 promote aggregation of the protein?
    • Shaw B.F., and Valentine J.S. How do ALS-associated mutations in superoxide dismutase 1 promote aggregation of the protein?. Trends Biochem. Sci. 32 (2007) 78-85
    • (2007) Trends Biochem. Sci. , vol.32 , pp. 78-85
    • Shaw, B.F.1    Valentine, J.S.2
  • 133
    • 0029079993 scopus 로고
    • Motor neuron disease caused by mutations in superoxide dismutase 1
    • Wong P.C., and Borchelt D.R. Motor neuron disease caused by mutations in superoxide dismutase 1. Curr. Opin. Neurol. 8 (1995) 294-301
    • (1995) Curr. Opin. Neurol. , vol.8 , pp. 294-301
    • Wong, P.C.1    Borchelt, D.R.2
  • 134
    • 0028960506 scopus 로고
    • Amyotrophic lateral sclerosis: recent insights from genetics and transgenic mice
    • Brown Jr. R.H. Amyotrophic lateral sclerosis: recent insights from genetics and transgenic mice. Cell 80 (1995) 687-692
    • (1995) Cell , vol.80 , pp. 687-692
    • Brown Jr., R.H.1
  • 135
    • 1842289165 scopus 로고    scopus 로고
    • Superoxide dismutase catalyzes nitration of tyrosines by peroxynitrite in the rod and head domains of neurofilament-L
    • Crow J.P., Ye Y.Z., Strong M., Kirk M., Barnes S., and Beckman J.S. Superoxide dismutase catalyzes nitration of tyrosines by peroxynitrite in the rod and head domains of neurofilament-L. J. Neurochem. 69 (1997) 1945-1953
    • (1997) J. Neurochem. , vol.69 , pp. 1945-1953
    • Crow, J.P.1    Ye, Y.Z.2    Strong, M.3    Kirk, M.4    Barnes, S.5    Beckman, J.S.6
  • 137
    • 0037059860 scopus 로고    scopus 로고
    • Bicarbonate enhances peroxidase activity of Cu,Zn-superoxide dismutase. Role of carbonate anion radical and scavenging of carbonate anion radical by metalloporphyrin antioxidant enzyme mimetics
    • Zhang H., Joseph J., Gurney M., Becker D., and Kalyanaraman B. Bicarbonate enhances peroxidase activity of Cu,Zn-superoxide dismutase. Role of carbonate anion radical and scavenging of carbonate anion radical by metalloporphyrin antioxidant enzyme mimetics. J. Biol. Chem. 277 (2002) 1013-1020
    • (2002) J. Biol. Chem. , vol.277 , pp. 1013-1020
    • Zhang, H.1    Joseph, J.2    Gurney, M.3    Becker, D.4    Kalyanaraman, B.5
  • 138
    • 0034530030 scopus 로고    scopus 로고
    • Oxidation versus aggregation - how do SOD1 mutants cause ALS?
    • Cleveland D.W., and Liu J. Oxidation versus aggregation - how do SOD1 mutants cause ALS?. Nat. Med. 6 (2000) 1320-1321
    • (2000) Nat. Med. , vol.6 , pp. 1320-1321
    • Cleveland, D.W.1    Liu, J.2
  • 139
    • 0021167918 scopus 로고
    • Fine structural observations of neurofilamentous changes in amyotrophic lateral sclerosis
    • Hirano A., Donnenfeld H., Sasaki S., and Nakano I. Fine structural observations of neurofilamentous changes in amyotrophic lateral sclerosis. J. Neuropathol. Exp. Neurol. 43 (1984) 461-470
    • (1984) J. Neuropathol. Exp. Neurol. , vol.43 , pp. 461-470
    • Hirano, A.1    Donnenfeld, H.2    Sasaki, S.3    Nakano, I.4
  • 140
    • 0033798660 scopus 로고    scopus 로고
    • Protein aggregation in Huntington's and Parkinson's disease: implications for therapy
    • Wanker E.E. Protein aggregation in Huntington's and Parkinson's disease: implications for therapy. Mol. Med. Today 6 (2000) 387-391
    • (2000) Mol. Med. Today , vol.6 , pp. 387-391
    • Wanker, E.E.1
  • 141
    • 0035827318 scopus 로고    scopus 로고
    • Protein misfolding and disease; protein refolding and therapy
    • Soto C. Protein misfolding and disease; protein refolding and therapy. FEBS Lett. 498 (2001) 204-207
    • (2001) FEBS Lett. , vol.498 , pp. 204-207
    • Soto, C.1
  • 142
    • 0030777650 scopus 로고    scopus 로고
    • Aggregation of mutant Cu/Zn superoxide dismutase proteins in a culture model of ALS
    • Durham H.D., Roy J., Dong L., and Figlewicz D.A. Aggregation of mutant Cu/Zn superoxide dismutase proteins in a culture model of ALS. J. Neuropathol. Exp. Neurol. 56 (1997) 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
  • 143
    • 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., Dalton M.J., Gurney M.E., and Kopito R.R. 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. U. S. A. 97 (2000) 12571-12576
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 12571-12576
    • Johnston, J.A.1    Dalton, M.J.2    Gurney, M.E.3    Kopito, R.R.4
  • 144
    • 0029927679 scopus 로고    scopus 로고
    • Intense superoxide dismutase-1 immunoreactivity in intracytoplasmic hyaline inclusions of familial amyotrophic lateral sclerosis with posterior column involvement
    • Shibata N., Hirano A., Kobayashi M., Siddique T., Deng H.X., Hung W.Y., Kato T., and Asayama K. Intense superoxide dismutase-1 immunoreactivity in intracytoplasmic hyaline inclusions of familial amyotrophic lateral sclerosis with posterior column involvement. J. Neuropathol. Exp. Neurol. 55 (1996) 481-490
    • (1996) J. Neuropathol. Exp. Neurol. , vol.55 , pp. 481-490
    • Shibata, N.1    Hirano, A.2    Kobayashi, M.3    Siddique, T.4    Deng, H.X.5    Hung, W.Y.6    Kato, T.7    Asayama, K.8
  • 145
    • 0034869733 scopus 로고    scopus 로고
    • Copper chaperone for superoxide dismutase co-aggregates with superoxide dismutase 1 (SOD1) in neuronal Lewy body-like hyaline inclusions: an immunohistochemical study on familial amyotrophic lateral sclerosis with SOD1 gene mutation
    • Kato S., Sumi-Akamaru H., Fujimura H., Sakoda S., Kato M., Hirano A., Takikawa M., and Ohama E. Copper chaperone for superoxide dismutase co-aggregates with superoxide dismutase 1 (SOD1) in neuronal Lewy body-like hyaline inclusions: an immunohistochemical study on familial amyotrophic lateral sclerosis with SOD1 gene mutation. Acta. Neuropathol. (Berl.) 102 (2001) 233-238
    • (2001) Acta. Neuropathol. (Berl.) , vol.102 , pp. 233-238
    • Kato, S.1    Sumi-Akamaru, H.2    Fujimura, H.3    Sakoda, S.4    Kato, M.5    Hirano, A.6    Takikawa, M.7    Ohama, E.8
  • 146
    • 0029991827 scopus 로고    scopus 로고
    • Colocalization of NOS and SOD1 in neurofilament accumulation within motor neurons of amyotrophic lateral sclerosis: an immunohistochemical study
    • Chou S.M., Wang H.S., and Komai K. Colocalization of NOS and SOD1 in neurofilament accumulation within motor neurons of amyotrophic lateral sclerosis: an immunohistochemical study. J. Chem. Neuroanat. 10 (1996) 249-258
    • (1996) J. Chem. Neuroanat. , vol.10 , pp. 249-258
    • Chou, S.M.1    Wang, H.S.2    Komai, K.3
  • 147
    • 0033971898 scopus 로고    scopus 로고
    • Mitochondria and neuronal survival
    • Nicholls D.G., and Budd S.L. Mitochondria and neuronal survival. Physiol. Rev. 80 (2000) 315-360
    • (2000) Physiol. Rev. , vol.80 , pp. 315-360
    • Nicholls, D.G.1    Budd, S.L.2
  • 148
    • 0034821922 scopus 로고    scopus 로고
    • CuZn superoxide dismutase (SOD1) accumulates in vacuolated mitochondria in transgenic mice expressing amyotrophic lateral sclerosis-linked SOD1 mutations
    • Jaarsma D., Rognoni F., van Duijn W., Verspaget H.W., Haasdijk E.D., and Holstege J.C. CuZn superoxide dismutase (SOD1) accumulates in vacuolated mitochondria in transgenic mice expressing amyotrophic lateral sclerosis-linked SOD1 mutations. Acta. Neuropathol. (Berl.) 102 (2001) 293-305
    • (2001) Acta. Neuropathol. (Berl.) , vol.102 , pp. 293-305
    • Jaarsma, D.1    Rognoni, F.2    van Duijn, W.3    Verspaget, H.W.4    Haasdijk, E.D.5    Holstege, J.C.6
  • 149
    • 0032079517 scopus 로고    scopus 로고
    • Massive mitochondrial degeneration in motor neurons triggers the onset of amyotrophic lateral sclerosis in mice expressing a mutant SOD1
    • Kong J., and Xu Z. Massive mitochondrial degeneration in motor neurons triggers the onset of amyotrophic lateral sclerosis in mice expressing a mutant SOD1. J. Neurosci. 18 (1998) 3241-3250
    • (1998) J. Neurosci. , vol.18 , pp. 3241-3250
    • Kong, J.1    Xu, Z.2
  • 150
    • 0035146334 scopus 로고    scopus 로고
    • Mitochondria-the suicide organelles
    • Ferri K.F., and Kroemer G. Mitochondria-the suicide organelles. BioEssays 23 (2001) 111-115
    • (2001) BioEssays , vol.23 , pp. 111-115
    • Ferri, K.F.1    Kroemer, G.2
  • 151
    • 0032430185 scopus 로고    scopus 로고
    • Caspase-1 is activated in neural cells and tissue with amyotrophic lateral sclerosis-associated mutations in copper-zinc superoxide dismutase [published erratum appears in Proc Natl Acad Sci U S A 1999 Mar 16;96(6):3330]
    • Pasinelli P., Borchelt D.R., Houseweart M.K., Cleveland D.W., and Brown Jr. R.H. Caspase-1 is activated in neural cells and tissue with amyotrophic lateral sclerosis-associated mutations in copper-zinc superoxide dismutase [published erratum appears in Proc Natl Acad Sci U S A 1999 Mar 16;96(6):3330]. Proc. Natl. Acad. Sci. U. S. A. 95 (1998) 15763-15768
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , pp. 15763-15768
    • Pasinelli, P.1    Borchelt, D.R.2    Houseweart, M.K.3    Cleveland, D.W.4    Brown Jr., R.H.5
  • 152
    • 0028915976 scopus 로고
    • Mutations associated with amyotrophic lateral sclerosis convert superoxide dismutase from an antiapoptotic gene to a proapoptotic gene: studies in yeast and neural cells
    • Rabizadeh S., Gralla E.B., Borchelt D.R., Gwinn R., Valentine J.S., Sisodia S., Wong P., Lee M., Hahn H., and Bredesen D.E. Mutations associated with amyotrophic lateral sclerosis convert superoxide dismutase from an antiapoptotic gene to a proapoptotic gene: studies in yeast and neural cells. Proc. Natl. Acad. Sci. U. S. A. 92 (1995) 3024-3028
    • (1995) Proc. Natl. Acad. Sci. U. S. A. , vol.92 , pp. 3024-3028
    • Rabizadeh, S.1    Gralla, E.B.2    Borchelt, D.R.3    Gwinn, R.4    Valentine, J.S.5    Sisodia, S.6    Wong, P.7    Lee, M.8    Hahn, H.9    Bredesen, D.E.10
  • 154
    • 0034610328 scopus 로고    scopus 로고
    • Caspase-1 and-3 are sequentially activated in motor neuron death in Cu,Zn superoxide dismutase-mediated familial amyotrophic lateral sclerosis
    • Pasinelli P., Houseweart M.K., Brown Jr. R.H., and Cleveland D.W. Caspase-1 and-3 are sequentially activated in motor neuron death in Cu,Zn superoxide dismutase-mediated familial amyotrophic lateral sclerosis. Proc. Natl. Acad. Sci. U. S. A. 97 (2000) 13901-13906
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 13901-13906
    • Pasinelli, P.1    Houseweart, M.K.2    Brown Jr., R.H.3    Cleveland, D.W.4
  • 155
    • 47549086869 scopus 로고    scopus 로고
    • Motor neuron disease: The curious ways of ALS
    • Polymenidou M., and Cleveland D.W. Motor neuron disease: The curious ways of ALS. Nature 454 (2008) 284-285
    • (2008) Nature , vol.454 , pp. 284-285
    • Polymenidou, M.1    Cleveland, D.W.2
  • 158
    • 3042616595 scopus 로고    scopus 로고
    • A membrane protein required for dislocation of misfolded proteins from the ER
    • Lilley B.N., and Ploegh H.L. A membrane protein required for dislocation of misfolded proteins from the ER. Nature 429 (2004) 834-840
    • (2004) Nature , vol.429 , pp. 834-840
    • Lilley, B.N.1    Ploegh, H.L.2
  • 160
    • 29444443348 scopus 로고    scopus 로고
    • Chromogranin-mediated secretion of mutant superoxide dismutase proteins linked to amyotrophic lateral sclerosis
    • Urushitani M., Sik A., Sakurai T., Nukina N., Takahashi R., and Julien J.P. Chromogranin-mediated secretion of mutant superoxide dismutase proteins linked to amyotrophic lateral sclerosis. Nat. Neurosci. 9 (2006) 108-118
    • (2006) Nat. Neurosci. , vol.9 , pp. 108-118
    • Urushitani, M.1    Sik, A.2    Sakurai, T.3    Nukina, N.4    Takahashi, R.5    Julien, J.P.6
  • 163
    • 34447550238 scopus 로고    scopus 로고
    • Interaction between familial amyotrophic lateral sclerosis (ALS)-linked SOD1 mutants and the dynein complex
    • Zhang F., Strom A.L., Fukada K., Lee S., Hayward L.J., and Zhu H. Interaction between familial amyotrophic lateral sclerosis (ALS)-linked SOD1 mutants and the dynein complex. J. Biol. Chem. 282 (2007) 16691-16699
    • (2007) J. Biol. Chem. , vol.282 , pp. 16691-16699
    • Zhang, F.1    Strom, A.L.2    Fukada, K.3    Lee, S.4    Hayward, L.J.5    Zhu, H.6
  • 165
    • 0022612089 scopus 로고
    • Recognition and interactions controlling the assemblies of beta barrel domains
    • Getzoff E.D., Tainer J.A., and Olson A.J. Recognition and interactions controlling the assemblies of beta barrel domains. Biophys. J. 49 (1986) 191-206
    • (1986) Biophys. J. , vol.49 , pp. 191-206
    • Getzoff, E.D.1    Tainer, J.A.2    Olson, A.J.3
  • 167
    • 37149049312 scopus 로고    scopus 로고
    • X-ray solution scattering (SAXS) combined with crystallography and computation: defining accurate macromolecular structures, conformations and assemblies in solution
    • Putnam C.D., Hammel M., Hura G.L., and Tainer J.A. X-ray solution scattering (SAXS) combined with crystallography and computation: defining accurate macromolecular structures, conformations and assemblies in solution. Q. Rev. Biophys. 40 (2007) 191-285
    • (2007) Q. Rev. Biophys. , vol.40 , pp. 191-285
    • Putnam, C.D.1    Hammel, M.2    Hura, G.L.3    Tainer, J.A.4
  • 170
    • 0021891901 scopus 로고
    • Structural analyses of various Cu2+, Zn2+-superoxide dismutases by differential scanning calorimetry and Raman spectroscopy
    • Lepock J.R., Arnold L.D., Torrie B.H., Andrews B., and Kruuv J. Structural analyses of various Cu2+, Zn2+-superoxide dismutases by differential scanning calorimetry and Raman spectroscopy. Arch. Biochem. Biophys. 241 (1985) 243-251
    • (1985) Arch. Biochem. Biophys. , vol.241 , pp. 243-251
    • Lepock, J.R.1    Arnold, L.D.2    Torrie, B.H.3    Andrews, B.4    Kruuv, J.5
  • 171
    • 0023862963 scopus 로고
    • Differential scanning calorimetry of Cu,Zn-superoxide dismutase, the apoprotein, and its zinc-substituted derivatives
    • Roe J.A., Butler A., Scholler D.M., Valentine J.S., Marky L., and Breslauer K.J. Differential scanning calorimetry of Cu,Zn-superoxide dismutase, the apoprotein, and its zinc-substituted derivatives. Biochemistry 27 (1988) 950-958
    • (1988) Biochemistry , vol.27 , pp. 950-958
    • Roe, J.A.1    Butler, A.2    Scholler, D.M.3    Valentine, J.S.4    Marky, L.5    Breslauer, K.J.6
  • 172
    • 0018789696 scopus 로고
    • Subunit association and side-chain reactivities of bovine erythrocyte superoxide dismutase in denaturing solvents
    • Malinowski D.P., and Fridovich I. Subunit association and side-chain reactivities of bovine erythrocyte superoxide dismutase in denaturing solvents. Biochemistry 18 (1979) 5055-5060
    • (1979) Biochemistry , vol.18 , pp. 5055-5060
    • Malinowski, D.P.1    Fridovich, I.2
  • 173
    • 0015935503 scopus 로고
    • On the stability of bovine superoxide dismutase. The effects of metals
    • Forman H.J., and Fridovich I. On the stability of bovine superoxide dismutase. The effects of metals. J. Biol. Chem. 248 (1973) 2645-2649
    • (1973) J. Biol. Chem. , vol.248 , pp. 2645-2649
    • Forman, H.J.1    Fridovich, I.2
  • 174
    • 84886620588 scopus 로고
    • Similarity of three-dimensional structure between the immunoglobulin domain and the copper, zinc superoxide dismutase subunit
    • Richardson J.S., Richardson D.C., Thomas K.A., Silverton E.W., and Davies D.R. Similarity of three-dimensional structure between the immunoglobulin domain and the copper, zinc superoxide dismutase subunit. J. Mol. Biol. 102 (1976) 221-235
    • (1976) J. Mol. Biol. , vol.102 , pp. 221-235
    • Richardson, J.S.1    Richardson, D.C.2    Thomas, K.A.3    Silverton, E.W.4    Davies, D.R.5
  • 175
    • 0042667013 scopus 로고    scopus 로고
    • Stereospecific interactions of proline residues in protein structures and complexes
    • Bhattacharyya R., and Chakrabarti P. Stereospecific interactions of proline residues in protein structures and complexes. J. Mol. Biol. 331 (2003) 925-940
    • (2003) J. Mol. Biol. , vol.331 , pp. 925-940
    • Bhattacharyya, R.1    Chakrabarti, P.2
  • 176
    • 0025074777 scopus 로고
    • Changes in crystallographic structure and thermostability of a Cu,Zn superoxide dismutase mutant resulting from the removal of a buried cysteine
    • McRee D.E., Redford S.M., Getzoff E.D., Lepock J.R., Hallewell R.A., and Tainer J.A. Changes in crystallographic structure and thermostability of a Cu,Zn superoxide dismutase mutant resulting from the removal of a buried cysteine. J. Biol. Chem. 265 (1990) 14234-14241
    • (1990) J. Biol. Chem. , vol.265 , pp. 14234-14241
    • McRee, D.E.1    Redford, S.M.2    Getzoff, E.D.3    Lepock, J.R.4    Hallewell, R.A.5    Tainer, J.A.6
  • 177
    • 0036440686 scopus 로고    scopus 로고
    • Insights into Lou Gehrig's disease from the structure and instability of the A4V mutant of human Cu,Zn superoxide dismutase
    • Cardoso R.M., Thayer M.M., DiDonato M., Lo T.P., Bruns C.K., Getzoff E.D., and Tainer J.A. Insights into Lou Gehrig's disease from the structure and instability of the A4V mutant of human Cu,Zn superoxide dismutase. J. Mol. Biol. 324 (2002) 247-256
    • (2002) J. Mol. Biol. , vol.324 , pp. 247-256
    • Cardoso, R.M.1    Thayer, M.M.2    DiDonato, M.3    Lo, T.P.4    Bruns, C.K.5    Getzoff, E.D.6    Tainer, J.A.7
  • 178
    • 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 Dokholyan N.V. Common dynamical signatures of familial amyotrophic lateral sclerosis-associated structurally diverse Cu, Zn superoxide dismutase mutants. Proc. Natl. Acad. Sci. U. S. A. 103 (2006) 3147-3152
    • (2006) Proc. Natl. Acad. Sci. U. S. A. , vol.103 , pp. 3147-3152
    • Khare, S.D.1    Dokholyan, N.V.2
  • 179
    • 0025667116 scopus 로고
    • Contribution of conformational stability and reversibility of unfolding to the increased thermostability of human and bovine superoxide dismutase mutated at free cysteines
    • Lepock J.R., Frey H.E., and Hallewell R.A. Contribution of conformational stability and reversibility of unfolding to the increased thermostability of human and bovine superoxide dismutase mutated at free cysteines. J. Biol. Chem. 265 (1990) 21612-21618
    • (1990) J. Biol. Chem. , vol.265 , pp. 21612-21618
    • Lepock, J.R.1    Frey, H.E.2    Hallewell, R.A.3
  • 181
    • 53049109088 scopus 로고    scopus 로고
    • Complete loss of post-translational modifications triggers fibrillar aggregation of SOD1 in the familial form of amyotrophic lateral sclerosis
    • Furukawa Y., Kaneko K., Yamanaka K., O'Halloran T.V., and Nukina N. Complete loss of post-translational modifications triggers fibrillar aggregation of SOD1 in the familial form of amyotrophic lateral sclerosis. J. Biol. Chem. 283 (2008) 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
  • 182
    • 0031911637 scopus 로고    scopus 로고
    • Subunit asymmetry in the three-dimensional structure of a human CuZnSOD mutant found in familial amyotrophic lateral sclerosis
    • Hart P.J., Liu H., Pellegrini M., Nersissian A.M., Gralla E.B., Valentine J.S., and Eisenberg D. Subunit asymmetry in the three-dimensional structure of a human CuZnSOD mutant found in familial amyotrophic lateral sclerosis. Protein. Sci. 7 (1998) 545-555
    • (1998) Protein. Sci. , vol.7 , pp. 545-555
    • Hart, P.J.1    Liu, H.2    Pellegrini, M.3    Nersissian, A.M.4    Gralla, E.B.5    Valentine, J.S.6    Eisenberg, D.7
  • 185
    • 0033166967 scopus 로고    scopus 로고
    • Unraveling the effect of changes in conformation and compactness at the antibody V(L)-V(H) interface upon antigen binding
    • Pellequer J.L., Chen S., Roberts V.A., Tainer J.A., and Getzoff E.D. Unraveling the effect of changes in conformation and compactness at the antibody V(L)-V(H) interface upon antigen binding. J. Mol. Recognit. 12 (1999) 267-275
    • (1999) J. Mol. Recognit. , vol.12 , pp. 267-275
    • Pellequer, J.L.1    Chen, S.2    Roberts, V.A.3    Tainer, J.A.4    Getzoff, E.D.5
  • 186
    • 0031015422 scopus 로고    scopus 로고
    • Prognosis in familial amyotrophic lateral sclerosis: progression and survival in patients with Glu100Gly and Ala4Val mutations in Cu,Zn superoxide dismutase
    • Juneja T., Pericak-Vance M.A., Laing N.G., Dave S., and Siddique T. Prognosis in familial amyotrophic lateral sclerosis: progression and survival in patients with Glu100Gly and Ala4Val mutations in Cu,Zn superoxide dismutase. Neurology 48 (1997) 55-57
    • (1997) Neurology , vol.48 , pp. 55-57
    • Juneja, T.1    Pericak-Vance, M.A.2    Laing, N.G.3    Dave, S.4    Siddique, T.5
  • 187
    • 0033829129 scopus 로고    scopus 로고
    • Expression and role of superoxide dismutases (SOD) in pathogenic bacteria
    • Lynch M., and Kuramitsu H. Expression and role of superoxide dismutases (SOD) in pathogenic bacteria. Microbes Infect. 2 (2000) 1245-1255
    • (2000) Microbes Infect. , vol.2 , pp. 1245-1255
    • Lynch, M.1    Kuramitsu, H.2
  • 188
    • 0023811053 scopus 로고
    • Normal oxidative damage to mitochondrial and nuclear DNA is extensive
    • Richter C., Park J., and Ames B.N. Normal oxidative damage to mitochondrial and nuclear DNA is extensive. Proc. Natl. Acad. Sci. U. S. A. 85 (1988) 6465-6467
    • (1988) Proc. Natl. Acad. Sci. U. S. A. , vol.85 , pp. 6465-6467
    • Richter, C.1    Park, J.2    Ames, B.N.3
  • 192
    • 0035503501 scopus 로고    scopus 로고
    • Lifespan extension and rescue of spongiform encephalopathy in superoxide dismutase 2 nullizygous mice treated with superoxide dismutase-catalase mimetics
    • Melov S., Doctrow S.R., Schneider J.A., Haberson J., Patel M., Coskun P.E., Huffman K., Wallace D.C., and Malfroy B. Lifespan extension and rescue of spongiform encephalopathy in superoxide dismutase 2 nullizygous mice treated with superoxide dismutase-catalase mimetics. J. Neurosci. 21 (2001) 8348-8353
    • (2001) J. Neurosci. , vol.21 , pp. 8348-8353
    • Melov, S.1    Doctrow, S.R.2    Schneider, J.A.3    Haberson, J.4    Patel, M.5    Coskun, P.E.6    Huffman, K.7    Wallace, D.C.8    Malfroy, B.9
  • 194
    • 0024292275 scopus 로고
    • Crystal structure of manganese superoxide dismutase from Bacillus stearothermophilus at 2.4 A resolution
    • Parker M.W., and Blake C.C. Crystal structure of manganese superoxide dismutase from Bacillus stearothermophilus at 2.4 A resolution. J. Mol. Biol. 199 (1988) 649-661
    • (1988) J. Mol. Biol. , vol.199 , pp. 649-661
    • Parker, M.W.1    Blake, C.C.2
  • 195
    • 0023851488 scopus 로고
    • Iron superoxide dismutase. Nucleotide sequence of the gene from Escherichia coli K12 and correlations with crystal structures
    • Carlioz A., Ludwig M.L., Stallings W.C., Fee J.A., Steinman H.M., and Touati D. Iron superoxide dismutase. Nucleotide sequence of the gene from Escherichia coli K12 and correlations with crystal structures. J. Biol. Chem. 263 (1988) 1555-1562
    • (1988) J. Biol. Chem. , vol.263 , pp. 1555-1562
    • Carlioz, A.1    Ludwig, M.L.2    Stallings, W.C.3    Fee, J.A.4    Steinman, H.M.5    Touati, D.6
  • 196
    • 0025847723 scopus 로고
    • Manganese superoxide dismutase from Thermus thermophilus. A structural model refined at 1.8 A resolution
    • Ludwig M.L., Metzger A.L., Pattridge K.A., and Stallings W.C. Manganese superoxide dismutase from Thermus thermophilus. A structural model refined at 1.8 A resolution. J. Mol. Biol. 219 (1991) 335-358
    • (1991) J. Mol. Biol. , vol.219 , pp. 335-358
    • Ludwig, M.L.1    Metzger, A.L.2    Pattridge, K.A.3    Stallings, W.C.4
  • 197
    • 0025196784 scopus 로고
    • The 2.1-A resolution structure of iron superoxide dismutase from Pseudomonas ovalis
    • Stoddard B.L., Howell P.L., Ringe D., and Petsko G.A. The 2.1-A resolution structure of iron superoxide dismutase from Pseudomonas ovalis. Biochemistry 29 (1990) 8885-8893
    • (1990) Biochemistry , vol.29 , pp. 8885-8893
    • Stoddard, B.L.1    Howell, P.L.2    Ringe, D.3    Petsko, G.A.4
  • 198
    • 0026688441 scopus 로고
    • The structure of human mitochondrial manganese superoxide dismutase reveals a novel tetrameric interface of two 4-helix bundles
    • Borgstahl G.E., Parge H.E., Hickey M.J., Beyer Jr. W.F., Hallewell R.A., and Tainer J.A. The structure of human mitochondrial manganese superoxide dismutase reveals a novel tetrameric interface of two 4-helix bundles. Cell 71 (1992) 107-118
    • (1992) Cell , vol.71 , pp. 107-118
    • Borgstahl, G.E.1    Parge, H.E.2    Hickey, M.J.3    Beyer Jr., W.F.4    Hallewell, R.A.5    Tainer, J.A.6
  • 199
    • 0028933323 scopus 로고
    • Structure-function in Escherichia coli iron superoxide dismutase: comparisons with the manganese enzyme from Thermus thermophilus
    • Lah M.S., Dixon M.M., Pattridge K.A., Stallings W.C., Fee J.A., and Ludwig M.L. Structure-function in Escherichia coli iron superoxide dismutase: comparisons with the manganese enzyme from Thermus thermophilus. Biochemistry 34 (1995) 1646-1660
    • (1995) Biochemistry , vol.34 , pp. 1646-1660
    • Lah, M.S.1    Dixon, M.M.2    Pattridge, K.A.3    Stallings, W.C.4    Fee, J.A.5    Ludwig, M.L.6
  • 200
    • 0027481686 scopus 로고
    • Comparison of the crystal structures of genetically engineered human manganese superoxide dismutase and manganese superoxide dismutase from Thermus thermophilus: differences in dimer-dimer interaction
    • Wagner U.G., Pattridge K.A., Ludwig M.L., Stallings W.C., Werber M.M., Oefner C., Frolow F., and Sussman J.L. Comparison of the crystal structures of genetically engineered human manganese superoxide dismutase and manganese superoxide dismutase from Thermus thermophilus: differences in dimer-dimer interaction. Protein Sci. 2 (1993) 814-825
    • (1993) Protein Sci. , vol.2 , pp. 814-825
    • Wagner, U.G.1    Pattridge, K.A.2    Ludwig, M.L.3    Stallings, W.C.4    Werber, M.M.5    Oefner, C.6    Frolow, F.7    Sussman, J.L.8
  • 202
    • 0037242288 scopus 로고    scopus 로고
    • The polymorphism of manganese superoxide dismutase is associated with diabetic nephropathy in Japanese type 2 diabetic patients
    • Nomiyama T., Tanaka Y., Piao L., Nagasaka K., Sakai K., Ogihara T., Nakajima K., Watada H., and Kawamori R. The polymorphism of manganese superoxide dismutase is associated with diabetic nephropathy in Japanese type 2 diabetic patients. J. Hum. Genet. 48 (2003) 138-141
    • (2003) J. Hum. Genet. , vol.48 , pp. 138-141
    • Nomiyama, T.1    Tanaka, Y.2    Piao, L.3    Nagasaka, K.4    Sakai, K.5    Ogihara, T.6    Nakajima, K.7    Watada, H.8    Kawamori, R.9
  • 204
    • 59349088582 scopus 로고    scopus 로고
    • The manganese superoxide dismutase Val16Ala polymorphism is associated with decreased risk of diabetic nephropathy in Chinese patients with type 2 diabetes
    • Liu L., Zheng T., Wang N., Wang F., Li M., Jiang J., Zhao R., Li L., Zhao W., Zhu Q., and Jia W. The manganese superoxide dismutase Val16Ala polymorphism is associated with decreased risk of diabetic nephropathy in Chinese patients with type 2 diabetes. Mol. Cell. Biochem. 322 (2009) 87-91
    • (2009) Mol. Cell. Biochem. , vol.322 , pp. 87-91
    • Liu, L.1    Zheng, T.2    Wang, N.3    Wang, F.4    Li, M.5    Jiang, J.6    Zhao, R.7    Li, L.8    Zhao, W.9    Zhu, Q.10    Jia, W.11
  • 205
    • 70350026896 scopus 로고    scopus 로고
    • Association between manganese superoxide dismutase (MnSOD) Val-9Ala polymorphism and cancer risk - a meta-analysis
    • Wang S., Wang F., Shi X., Dai J., Peng Y., Guo X., Wang X., Shen H., and Hu Z. Association between manganese superoxide dismutase (MnSOD) Val-9Ala polymorphism and cancer risk - a meta-analysis. Eur. J. Cancer. 48 16 (2009) 2874-2881
    • (2009) Eur. J. Cancer. , vol.48 , Issue.16 , pp. 2874-2881
    • Wang, S.1    Wang, F.2    Shi, X.3    Dai, J.4    Peng, Y.5    Guo, X.6    Wang, X.7    Shen, H.8    Hu, Z.9
  • 206
    • 63049084598 scopus 로고    scopus 로고
    • MnSOD genotype and prostate cancer risk as a function of NAT genotype and smoking status
    • Iguchi T., Sugita S., Wang C.Y., Newman N.B., Nakatani T., and Haas G.P. MnSOD genotype and prostate cancer risk as a function of NAT genotype and smoking status. In Vivo 23 (2009) 7-12
    • (2009) In Vivo , vol.23 , pp. 7-12
    • Iguchi, T.1    Sugita, S.2    Wang, C.Y.3    Newman, N.B.4    Nakatani, T.5    Haas, G.P.6
  • 207
    • 58249141334 scopus 로고    scopus 로고
    • Association between manganese superoxide dismutase polymorphism and risk of lung cancer
    • Zejnilovic J., Akev N., Yilmaz H., and Isbir T. Association between manganese superoxide dismutase polymorphism and risk of lung cancer. Cancer Genet. Cytogenet. 189 (2009) 1-4
    • (2009) Cancer Genet. Cytogenet. , vol.189 , pp. 1-4
    • Zejnilovic, J.1    Akev, N.2    Yilmaz, H.3    Isbir, T.4
  • 208
    • 55749114380 scopus 로고    scopus 로고
    • Additive effect between quinine oxidoreductase gene (NQO1: Pro187Ser) and manganese superoxide dismutase gene (MnSOD: Ala-9Val) polymorphisms on tardive dyskinesia in patients with schizophrenia
    • Pae C.U. Additive effect between quinine oxidoreductase gene (NQO1: Pro187Ser) and manganese superoxide dismutase gene (MnSOD: Ala-9Val) polymorphisms on tardive dyskinesia in patients with schizophrenia. Psychiatry Res. 161 (2008) 336-338
    • (2008) Psychiatry Res. , vol.161 , pp. 336-338
    • Pae, C.U.1
  • 209
    • 57349088677 scopus 로고    scopus 로고
    • Manganese superoxide dismutase (MnSOD) gene polymorphism, interactions with carotenoid levels and prostate cancer risk
    • Mikhak B., Hunter D.J., Spiegelman D., Platz E.A., Wu K., Erdman Jr. J.W., and Giovannucci E. Manganese superoxide dismutase (MnSOD) gene polymorphism, interactions with carotenoid levels and prostate cancer risk. Carcinogenesis 29 (2008) 2335-2340
    • (2008) Carcinogenesis , vol.29 , pp. 2335-2340
    • Mikhak, B.1    Hunter, D.J.2    Spiegelman, D.3    Platz, E.A.4    Wu, K.5    Erdman Jr., J.W.6    Giovannucci, E.7
  • 212
    • 0000867630 scopus 로고
    • Brownian dynamics simulation of the superoxide-superoxide dismutase reaction: iron and manganse enzymes
    • Sines J., Allison S., Wierzbicki A., and McCammon J.A. Brownian dynamics simulation of the superoxide-superoxide dismutase reaction: iron and manganse enzymes. J. Phys. Chem. 94 (1990) 959-961
    • (1990) J. Phys. Chem. , vol.94 , pp. 959-961
    • Sines, J.1    Allison, S.2    Wierzbicki, A.3    McCammon, J.A.4
  • 213
    • 0035807030 scopus 로고    scopus 로고
    • Redox properties of human manganese superoxide dismutase and active-site mutants
    • Leveque V.J., Vance C.K., Nick H.S., and Silverman D.N. Redox properties of human manganese superoxide dismutase and active-site mutants. Biochemistry 40 (2001) 10586-10591
    • (2001) Biochemistry , vol.40 , pp. 10586-10591
    • Leveque, V.J.1    Vance, C.K.2    Nick, H.S.3    Silverman, D.N.4
  • 214
    • 0028938504 scopus 로고
    • X-ray absorption spectroscopy of the iron site in Escherichia coli Fe(III) superoxide dismutase
    • Tierney D.L., Fee J.A., Ludwig M.L., and Penner-Hahn J.E. X-ray absorption spectroscopy of the iron site in Escherichia coli Fe(III) superoxide dismutase. Biochemistry 34 (1995) 1661-1668
    • (1995) Biochemistry , vol.34 , pp. 1661-1668
    • Tierney, D.L.1    Fee, J.A.2    Ludwig, M.L.3    Penner-Hahn, J.E.4
  • 215
    • 0029944136 scopus 로고    scopus 로고
    • Low-temperature thermochromism marks a change in coordination for the metal ion in manganese superoxide dismutase
    • Whittaker M.M., and Whittaker J.W. Low-temperature thermochromism marks a change in coordination for the metal ion in manganese superoxide dismutase. Biochemistry 35 (1996) 6762-6770
    • (1996) Biochemistry , vol.35 , pp. 6762-6770
    • Whittaker, M.M.1    Whittaker, J.W.2
  • 216
    • 0019880897 scopus 로고
    • Saturation behavior of superoxide dismutation catalyzed by the iron containing superoxide dismutase of E. coli B
    • Fee J.A., McClune G.J., O'Neill P., and Fielden E.M. Saturation behavior of superoxide dismutation catalyzed by the iron containing superoxide dismutase of E. coli B. Biochem. Biophys. Res. Commun. 100 (1981) 377-384
    • (1981) Biochem. Biophys. Res. Commun. , vol.100 , pp. 377-384
    • Fee, J.A.1    McClune, G.J.2    O'Neill, P.3    Fielden, E.M.4
  • 217
    • 0020730787 scopus 로고
    • Electrostatic facilitation of the reaction catalyzed by the manganese-containing and the iron-containing superoxide dismutases
    • Benovic J., Tillman T., Cudd A., and Fridovich I. Electrostatic facilitation of the reaction catalyzed by the manganese-containing and the iron-containing superoxide dismutases. Arch. Biochem. Biophys. 221 (1983) 329-332
    • (1983) Arch. Biochem. Biophys. , vol.221 , pp. 329-332
    • Benovic, J.1    Tillman, T.2    Cudd, A.3    Fridovich, I.4
  • 218
    • 17644424319 scopus 로고    scopus 로고
    • Anion binding properties of reduced and oxidized iron-containing superoxide dismutase reveal no requirement for tyrosine 34
    • Miller A.F., Sorkin D.L., and Padmakumar K. Anion binding properties of reduced and oxidized iron-containing superoxide dismutase reveal no requirement for tyrosine 34. Biochemistry 44 (2005) 5969-5981
    • (2005) Biochemistry , vol.44 , pp. 5969-5981
    • Miller, A.F.1    Sorkin, D.L.2    Padmakumar, K.3
  • 219
    • 0000755267 scopus 로고
    • Kinetic-studies of superoxide dismutasese: properties of the manganese-containing protein from Thermus-thermophilus
    • Bull C.N., Yoshida T., and Fee J.A. Kinetic-studies of superoxide dismutasese: properties of the manganese-containing protein from Thermus-thermophilus. J. Am. Chem. Soc. 113 (1991) 4069-4076
    • (1991) J. Am. Chem. Soc. , vol.113 , pp. 4069-4076
    • Bull, C.N.1    Yoshida, T.2    Fee, J.A.3
  • 220
    • 13444257644 scopus 로고    scopus 로고
    • Probing the geometric and electronic structures of the low-temperature azide adduct and the product-inhibited form of oxidized manganese superoxide dismutase
    • Jackson T.A., Karapetian A., Miller A.F., and Brunold T.C. Probing the geometric and electronic structures of the low-temperature azide adduct and the product-inhibited form of oxidized manganese superoxide dismutase. Biochemistry 44 (2005) 1504-1520
    • (2005) Biochemistry , vol.44 , pp. 1504-1520
    • Jackson, T.A.1    Karapetian, A.2    Miller, A.F.3    Brunold, T.C.4
  • 221
    • 0036125438 scopus 로고    scopus 로고
    • Catalytic pathway of manganese superoxide dismutase by direct observation of superoxide
    • Silverman D.N., and Nick H.S. Catalytic pathway of manganese superoxide dismutase by direct observation of superoxide. Methods. Enzymol. 349 (2002) 61-74
    • (2002) Methods. Enzymol. , vol.349 , pp. 61-74
    • Silverman, D.N.1    Nick, H.S.2
  • 223
    • 0040186069 scopus 로고    scopus 로고
    • Multiple replacements of glutamine 143 in human manganese superoxide dismutase: effects on structure, stability, and catalysis
    • Leveque V.J., Stroupe M.E., Lepock J.R., Cabelli D.E., Tainer J.A., Nick H.S., and Silverman D.N. Multiple replacements of glutamine 143 in human manganese superoxide dismutase: effects on structure, stability, and catalysis. Biochemistry 39 (2000) 7131-7137
    • (2000) Biochemistry , vol.39 , pp. 7131-7137
    • Leveque, V.J.1    Stroupe, M.E.2    Lepock, J.R.3    Cabelli, D.E.4    Tainer, J.A.5    Nick, H.S.6    Silverman, D.N.7
  • 224
    • 0347926494 scopus 로고    scopus 로고
    • Catalytic and structural effects of amino acid substitution at histidine 30 in human manganese superoxide dismutase: insertion of valine C gamma into the substrate access channel
    • Hearn A.S., Stroupe M.E., Cabelli D.E., Ramilo C.A., Luba J.P., Tainer J.A., Nick H.S., and Silverman D.N. Catalytic and structural effects of amino acid substitution at histidine 30 in human manganese superoxide dismutase: insertion of valine C gamma into the substrate access channel. Biochemistry 42 (2003) 2781-2789
    • (2003) Biochemistry , vol.42 , pp. 2781-2789
    • Hearn, A.S.1    Stroupe, M.E.2    Cabelli, D.E.3    Ramilo, C.A.4    Luba, J.P.5    Tainer, J.A.6    Nick, H.S.7    Silverman, D.N.8
  • 228
    • 31344443566 scopus 로고    scopus 로고
    • Crystal structure of nitrated human manganese superoxide dismutase: mechanism of inactivation
    • Quint P., Reutzel R., Mikulski R., McKenna R., and Silverman D.N. Crystal structure of nitrated human manganese superoxide dismutase: mechanism of inactivation. Free Radic. Biol. Med. 40 (2006) 453-458
    • (2006) Free Radic. Biol. Med. , vol.40 , pp. 453-458
    • Quint, P.1    Reutzel, R.2    Mikulski, R.3    McKenna, R.4    Silverman, D.N.5
  • 229
    • 33745185969 scopus 로고    scopus 로고
    • Kinetic and structural characterization of human manganese superoxide dismutase containing 3-fluorotyrosines
    • Ren X., Tu C., Bhatt D., Perry J.J.P., Tainer J.A., Cabelli D.E., and Silverman D.N. Kinetic and structural characterization of human manganese superoxide dismutase containing 3-fluorotyrosines. J. Mol. Struct. 790 (2006) 168-173
    • (2006) J. Mol. Struct. , vol.790 , pp. 168-173
    • Ren, X.1    Tu, C.2    Bhatt, D.3    Perry, J.J.P.4    Tainer, J.A.5    Cabelli, D.E.6    Silverman, D.N.7
  • 231
    • 65249133409 scopus 로고    scopus 로고
    • Contribution of human manganese superoxide dismutase tyrosine 34 to structure and catalysis
    • Perry J.J., Hearn A.S., Cabelli D.E., Nick H.S., Tainer J.A., and Silverman D.N. Contribution of human manganese superoxide dismutase tyrosine 34 to structure and catalysis. Biochemistry 48 (2009) 3417-3424
    • (2009) Biochemistry , vol.48 , pp. 3417-3424
    • Perry, J.J.1    Hearn, A.S.2    Cabelli, D.E.3    Nick, H.S.4    Tainer, J.A.5    Silverman, D.N.6
  • 232
    • 0036119040 scopus 로고    scopus 로고
    • Prokaryotic manganese superoxide dismutases
    • Whittaker J.W. Prokaryotic manganese superoxide dismutases. Methods. Enzymol. 349 (2002) 80-90
    • (2002) Methods. Enzymol. , vol.349 , pp. 80-90
    • Whittaker, J.W.1
  • 233
    • 0023945399 scopus 로고
    • Iron-and manganese-containing superoxide dismutases can be distinguished by analysis of their primary structures
    • Parker M.W., and Blake C.C. Iron-and manganese-containing superoxide dismutases can be distinguished by analysis of their primary structures. FEBS Lett. 229 (1988) 377-382
    • (1988) FEBS Lett. , vol.229 , pp. 377-382
    • Parker, M.W.1    Blake, C.C.2
  • 235
    • 0028852868 scopus 로고
    • The pH-dependent changes of the enzymic activity and spectroscopic properties of iron-substituted manganese superoxide dismutase. A study on the metal-specific activity of Mn-containing superoxide dismutase
    • Yamakura F., Kobayashi K., Ue H., and Konno M. The pH-dependent changes of the enzymic activity and spectroscopic properties of iron-substituted manganese superoxide dismutase. A study on the metal-specific activity of Mn-containing superoxide dismutase. Eur. J. Biochem. 227 (1995) 700-706
    • (1995) Eur. J. Biochem. , vol.227 , pp. 700-706
    • Yamakura, F.1    Kobayashi, K.2    Ue, H.3    Konno, M.4
  • 236
    • 0030860007 scopus 로고    scopus 로고
    • Mutagenesis of a proton linkage pathway in Escherichia coli manganese superoxide dismutase
    • Whittaker M.M., and Whittaker J.W. Mutagenesis of a proton linkage pathway in Escherichia coli manganese superoxide dismutase. Biochemistry 36 (1997) 8923-8931
    • (1997) Biochemistry , vol.36 , pp. 8923-8931
    • Whittaker, M.M.1    Whittaker, J.W.2
  • 237
    • 0032560945 scopus 로고    scopus 로고
    • Distinct metal environment in Fe-substituted manganese superoxide dismutase provides a structural basis of metal specificity
    • Edwards R.A., Whittaker M.M., Whittaker J.W., Jameson G.B., and Baker E.N. Distinct metal environment in Fe-substituted manganese superoxide dismutase provides a structural basis of metal specificity. J. Am. Chem. Soc. 120 (1998) 9684-9685
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 9684-9685
    • Edwards, R.A.1    Whittaker, M.M.2    Whittaker, J.W.3    Jameson, G.B.4    Baker, E.N.5
  • 238
    • 0032554625 scopus 로고    scopus 로고
    • Spectroscopic comparisons of the pH dependencies of Fe-substituted (Mn)superoxide dismutase and Fe-superoxide dismutase
    • Vance C.K., and Miller A.F. Spectroscopic comparisons of the pH dependencies of Fe-substituted (Mn)superoxide dismutase and Fe-superoxide dismutase. Biochemistry 37 (1998) 5518-5527
    • (1998) Biochemistry , vol.37 , pp. 5518-5527
    • Vance, C.K.1    Miller, A.F.2
  • 239
    • 0023030627 scopus 로고
    • A Streptococcus mutans superoxide dismutase that is active with either manganese or iron as a cofactor
    • Martin M.E., Byers B.R., Olson M.O., Salin M.L., Arceneaux J.E., and Tolbert C. A Streptococcus mutans superoxide dismutase that is active with either manganese or iron as a cofactor. J. Biol. Chem. 261 (1986) 9361-9367
    • (1986) J. Biol. Chem. , vol.261 , pp. 9361-9367
    • Martin, M.E.1    Byers, B.R.2    Olson, M.O.3    Salin, M.L.4    Arceneaux, J.E.5    Tolbert, C.6
  • 240
    • 0033920250 scopus 로고    scopus 로고
    • Crystal structure of cambialistic superoxide dismutase from porphyromonas gingivalis
    • Sugio S., Hiraoka B.Y., and Yamakura F. Crystal structure of cambialistic superoxide dismutase from porphyromonas gingivalis. Eur. J. Biochem. 267 (2000) 3487-3495
    • (2000) Eur. J. Biochem. , vol.267 , pp. 3487-3495
    • Sugio, S.1    Hiraoka, B.Y.2    Yamakura, F.3
  • 242
    • 33750058553 scopus 로고    scopus 로고
    • Engineering and characterization of human manganese superoxide dismutase mutants with high activity and low product inhibition
    • Chockalingam K., Luba J., Nick H.S., Silverman D.N., and Zhao H. Engineering and characterization of human manganese superoxide dismutase mutants with high activity and low product inhibition. FEBS J. 273 (2006) 4853-4861
    • (2006) FEBS J. , vol.273 , pp. 4853-4861
    • Chockalingam, K.1    Luba, J.2    Nick, H.S.3    Silverman, D.N.4    Zhao, H.5
  • 244
    • 34547673497 scopus 로고    scopus 로고
    • Peroxynitrite: biochemistry pathophysiology and development of therapeutics
    • Szabo C., Ischiropoulos H., and Radi R. Peroxynitrite: biochemistry pathophysiology and development of therapeutics. Nat. Rev. Drug Discovery 6 (2007) 662-680
    • (2007) Nat. Rev. Drug Discovery , vol.6 , pp. 662-680
    • Szabo, C.1    Ischiropoulos, H.2    Radi, R.3
  • 245
    • 0025189864 scopus 로고
    • Apparent hydroxyl radical production by peroxynitrite: implications for endothelial injury from nitric oxide and superoxide
    • Beckman J.S., Beckman T.W., Chen J., Marshall P.A., and Freeman B.A. Apparent hydroxyl radical production by peroxynitrite: implications for endothelial injury from nitric oxide and superoxide. Proc. Natl. Acad. Sci. U. S. A. 87 (1990) 1620-1624
    • (1990) Proc. Natl. Acad. Sci. U. S. A. , vol.87 , pp. 1620-1624
    • Beckman, J.S.1    Beckman, T.W.2    Chen, J.3    Marshall, P.A.4    Freeman, B.A.5
  • 246
    • 34250714956 scopus 로고    scopus 로고
    • Biochemistry of protein tyrosine nitration in cardiovascular pathology
    • Peluffo G., and Radi R. Biochemistry of protein tyrosine nitration in cardiovascular pathology. Cardiovasc. Res. 75 (2007) 291-302
    • (2007) Cardiovasc. Res. , vol.75 , pp. 291-302
    • Peluffo, G.1    Radi, R.2
  • 247
    • 0029778889 scopus 로고    scopus 로고
    • A novel nickel-containing superoxide dismutase from Streptomyces spp
    • Youn H.D., Kim E.J., Roe J.H., Hah Y.C., and Kang S.O. A novel nickel-containing superoxide dismutase from Streptomyces spp. Biochem. J. 318 Pt. 3 (1996) 889-896
    • (1996) Biochem. J. , vol.318 , Issue.PART 3 , pp. 889-896
    • Youn, H.D.1    Kim, E.J.2    Roe, J.H.3    Hah, Y.C.4    Kang, S.O.5
  • 250
    • 62449124555 scopus 로고    scopus 로고
    • In silico analysis of nickel containing superoxide dismutase evolution and regulation
    • Schmidt A., Gube M., and Kothe E. In silico analysis of nickel containing superoxide dismutase evolution and regulation. J. Basic Microbiol. 49 (2009) 109-118
    • (2009) J. Basic Microbiol. , vol.49 , pp. 109-118
    • Schmidt, A.1    Gube, M.2    Kothe, E.3
  • 254
    • 0031962963 scopus 로고    scopus 로고
    • Transcriptional and post-transcriptional regulation by nickel of sodN gene encoding nickel-containing superoxide dismutase from Streptomyces coelicolor Muller
    • Kim E.J., Chung H.J., Suh B., Hah Y.C., and Roe J.H. Transcriptional and post-transcriptional regulation by nickel of sodN gene encoding nickel-containing superoxide dismutase from Streptomyces coelicolor Muller. Mol. Microbiol. 27 (1998) 187-195
    • (1998) Mol. Microbiol. , vol.27 , pp. 187-195
    • Kim, E.J.1    Chung, H.J.2    Suh, B.3    Hah, Y.C.4    Roe, J.H.5
  • 255
    • 0025929954 scopus 로고
    • Advances in the understanding of the structure-function relationship in Cu,Zn superoxide dismutase
    • Banci L., Bertini I., Cabelli D.E., Hallewell R.A., Luchinat C., and Viezzoli M.S. Advances in the understanding of the structure-function relationship in Cu,Zn superoxide dismutase. Free Radic. Res. Commun. 12-13 Pt 1 (1991) 239-251
    • (1991) Free Radic. Res. Commun. , vol.12-13 , Issue.PART 1 , pp. 239-251
    • Banci, L.1    Bertini, I.2    Cabelli, D.E.3    Hallewell, R.A.4    Luchinat, C.5    Viezzoli, M.S.6
  • 256
    • 0037248891 scopus 로고    scopus 로고
    • Proton-coupled electron transfer in Fe-superoxide dismutase and Mn-superoxide dismutase
    • Miller A.F., Padmakumar K., Sorkin D.L., Karapetian A., and Vance C.K. Proton-coupled electron transfer in Fe-superoxide dismutase and Mn-superoxide dismutase. J. Inorg. Biochem. 93 (2003) 71-83
    • (2003) J. Inorg. Biochem. , vol.93 , pp. 71-83
    • Miller, A.F.1    Padmakumar, K.2    Sorkin, D.L.3    Karapetian, A.4    Vance, C.K.5
  • 258
    • 0030888269 scopus 로고    scopus 로고
    • The conserved residue tyrosine 34 is essential for maximal activity of iron-superoxide dismutase from Escherichia coli
    • Hunter T., Ikebukuro K., Bannister W.H., Bannister J.V., and Hunter G.J. The conserved residue tyrosine 34 is essential for maximal activity of iron-superoxide dismutase from Escherichia coli. Biochemistry 36 (1997) 4925-4933
    • (1997) Biochemistry , vol.36 , pp. 4925-4933
    • Hunter, T.1    Ikebukuro, K.2    Bannister, W.H.3    Bannister, J.V.4    Hunter, G.J.5
  • 259
    • 0011509370 scopus 로고    scopus 로고
    • structural and functional aspects of metal sites in biology
    • Holm R.H., Kennepohl P., and Solomon E.I. structural and functional aspects of metal sites in biology. Chem. Rev. 96 (1996) 2239-2314
    • (1996) Chem. Rev. , vol.96 , pp. 2239-2314
    • Holm, R.H.1    Kennepohl, P.2    Solomon, E.I.3
  • 260
    • 43649098548 scopus 로고    scopus 로고
    • Redox tuning over almost 1 V in a structurally conserved active site: lessons from Fe-containing superoxide dismutase
    • Miller A.F. Redox tuning over almost 1 V in a structurally conserved active site: lessons from Fe-containing superoxide dismutase. Acc. Chem. Res. 41 (2008) 501-510
    • (2008) Acc. Chem. Res. , vol.41 , pp. 501-510
    • Miller, A.F.1
  • 261
    • 0033120016 scopus 로고    scopus 로고
    • Structure/function relationships in nickel metallobiochemistry
    • Maroney M.J. Structure/function relationships in nickel metallobiochemistry. Curr. Opin. Chem. Biol. 3 (1999) 188-199
    • (1999) Curr. Opin. Chem. Biol. , vol.3 , pp. 188-199
    • Maroney, M.J.1
  • 262
    • 17644414093 scopus 로고    scopus 로고
    • Spectroscopic and computational studies of Ni superoxide dismutase: electronic structure contributions to enzymatic function
    • Fiedler A.T., Bryngelson P.A., Maroney M.J., and Brunold T.C. Spectroscopic and computational studies of Ni superoxide dismutase: electronic structure contributions to enzymatic function. J. Am. Chem. Soc. 127 (2005) 5449-5462
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 5449-5462
    • Fiedler, A.T.1    Bryngelson, P.A.2    Maroney, M.J.3    Brunold, T.C.4
  • 263
    • 33745078745 scopus 로고    scopus 로고
    • Nickel superoxide dismutase reaction mechanism studied by hybrid density functional methods
    • Pelmenschikov V., and Siegbahn P.E. Nickel superoxide dismutase reaction mechanism studied by hybrid density functional methods. J. Am. Chem. Soc. 128 (2006) 7466-7475
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 7466-7475
    • Pelmenschikov, V.1    Siegbahn, P.E.2
  • 265
    • 58449126592 scopus 로고    scopus 로고
    • New insight into the mode of action of nickel superoxide dismutase by investigating metallopeptide substrate models
    • Tietze D., Breitzke H., Imhof D., Kothe E., Weston J., and Buntkowsky G. New insight into the mode of action of nickel superoxide dismutase by investigating metallopeptide substrate models. Chemistry 15 (2009) 517-523
    • (2009) Chemistry , vol.15 , pp. 517-523
    • Tietze, D.1    Breitzke, H.2    Imhof, D.3    Kothe, E.4    Weston, J.5    Buntkowsky, G.6
  • 267
    • 37549027250 scopus 로고    scopus 로고
    • Metal-catalyzed oxidation of the Werner syndrome protein causes loss of catalytic activities and impaired protein-protein interactions
    • Harrigan J.A., Piotrowski J., Di Noto L., Levine R.L., and Bohr V.A. Metal-catalyzed oxidation of the Werner syndrome protein causes loss of catalytic activities and impaired protein-protein interactions. J. Biol. Chem. 282 (2007) 36403-36411
    • (2007) J. Biol. Chem. , vol.282 , pp. 36403-36411
    • Harrigan, J.A.1    Piotrowski, J.2    Di Noto, L.3    Levine, R.L.4    Bohr, V.A.5
  • 269
    • 0032545515 scopus 로고    scopus 로고
    • Werner syndrome protein. I. DNA helicase and dna exonuclease reside on the same polypeptide
    • Shen J.C., Gray M.D., Oshima J., Kamath-Loeb A.S., Fry M., and Loeb L.A. Werner syndrome protein. I. DNA helicase and dna exonuclease reside on the same polypeptide. J. Biol. Chem. 273 (1998) 34139-34144
    • (1998) J. Biol. Chem. , vol.273 , pp. 34139-34144
    • Shen, J.C.1    Gray, M.D.2    Oshima, J.3    Kamath-Loeb, A.S.4    Fry, M.5    Loeb, L.A.6
  • 270
    • 56449090762 scopus 로고    scopus 로고
    • Rising from the RecQ-age: the role of human RecQ helicases in genome maintenance
    • Bohr V.A. Rising from the RecQ-age: the role of human RecQ helicases in genome maintenance. Trends Biochem. Sci. 33 (2008) 609-620
    • (2008) Trends Biochem. Sci. , vol.33 , pp. 609-620
    • Bohr, V.A.1
  • 271
    • 58149235463 scopus 로고    scopus 로고
    • Werner Syndrome, aging and cancer
    • Ozgenc A., and Loeb L.A. Werner Syndrome, aging and cancer. Genome Dyn. 1 (2006) 206-217
    • (2006) Genome Dyn. , vol.1 , pp. 206-217
    • Ozgenc, A.1    Loeb, L.A.2
  • 274
    • 0027940508 scopus 로고
    • Molecular mechanisms of damage by excess nitrogen oxides: nitration of tyrosine by gas-phase cigarette smoke
    • Eiserich J.P., Vossen V., O'Neill C.A., Halliwell B., Cross C.E., and van der Vliet A. Molecular mechanisms of damage by excess nitrogen oxides: nitration of tyrosine by gas-phase cigarette smoke. FEBS Lett. 353 (1994) 53-56
    • (1994) FEBS Lett. , vol.353 , pp. 53-56
    • Eiserich, J.P.1    Vossen, V.2    O'Neill, C.A.3    Halliwell, B.4    Cross, C.E.5    van der Vliet, A.6
  • 275
    • 0028584148 scopus 로고
    • Reactions of nitric oxide, superoxide and peroxynitrite with superoxide dismutase in neurodegeneration
    • Beckman J.S., Chen J., Crow J.P., and Ye Y.Z. Reactions of nitric oxide, superoxide and peroxynitrite with superoxide dismutase in neurodegeneration. Prog. Brain Res. 103 (1994) 371-380
    • (1994) Prog. Brain Res. , vol.103 , pp. 371-380
    • Beckman, J.S.1    Chen, J.2    Crow, J.P.3    Ye, Y.Z.4
  • 276
    • 0027319341 scopus 로고
    • Cytotoxicity and genotoxicity of lipid-oxidation products
    • discussion 785S-786S
    • Esterbauer H. Cytotoxicity and genotoxicity of lipid-oxidation products. Am. J. Clin. Nutr. 57 (1993) 779S-785S discussion 785S-786S
    • (1993) Am. J. Clin. Nutr. , vol.57
    • Esterbauer, H.1
  • 277
    • 0026775958 scopus 로고
    • Free radical theory of aging
    • Harman D. Free radical theory of aging. Mutat. Res. 275 (1992) 257-266
    • (1992) Mutat. Res. , vol.275 , pp. 257-266
    • Harman, D.1
  • 279
    • 44149094083 scopus 로고    scopus 로고
    • XPD helicase structures and activities: insights into the cancer and aging phenotypes from XPD mutations
    • Fan L., Fuss J.O., Cheng Q.J., Arvai A.S., Hammel M., Roberts V.A., Cooper P.K., and Tainer J.A. XPD helicase structures and activities: insights into the cancer and aging phenotypes from XPD mutations. Cell 133 (2008) 789-800
    • (2008) Cell , vol.133 , pp. 789-800
    • Fan, L.1    Fuss, J.O.2    Cheng, Q.J.3    Arvai, A.S.4    Hammel, M.5    Roberts, V.A.6    Cooper, P.K.7    Tainer, J.A.8
  • 282
    • 48349137105 scopus 로고    scopus 로고
    • The threat of instability: neurodegeneration predicted by protein destabilization and aggregation propensity
    • Meiering E.M. The threat of instability: neurodegeneration predicted by protein destabilization and aggregation propensity. PLoS Biol. 6 (2008) e193
    • (2008) PLoS Biol. , vol.6
    • Meiering, E.M.1
  • 283
    • 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., and Dobson C.M. Rationalization of the effects of mutations on peptide and protein aggregation rates. Nature 424 (2003) 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
  • 284
    • 22244479388 scopus 로고    scopus 로고
    • Copper-zinc superoxide dismutase and amyotrophic lateral sclerosis
    • Valentine J.S., Doucette P.A., and Zittin Potter S. Copper-zinc superoxide dismutase and amyotrophic lateral sclerosis. Annu. Rev. Biochem. 74 (2005) 563-593
    • (2005) Annu. Rev. Biochem. , vol.74 , pp. 563-593
    • Valentine, J.S.1    Doucette, P.A.2    Zittin Potter, S.3
  • 286
    • 0024375781 scopus 로고
    • Oxygen radicals in influenza-induced pathogenesis and treatment with pyran polymer-conjugated SOD
    • Oda T., Akaike T., Hamamoto T., Suzuki F., Hirano T., and Maeda H. Oxygen radicals in influenza-induced pathogenesis and treatment with pyran polymer-conjugated SOD. Science 244 (1989) 974-976
    • (1989) Science , vol.244 , pp. 974-976
    • Oda, T.1    Akaike, T.2    Hamamoto, T.3    Suzuki, F.4    Hirano, T.5    Maeda, H.6
  • 288
    • 30344461640 scopus 로고    scopus 로고
    • The induction of human superoxide dismutase and catalase in vivo: a fundamentally new approach to antioxidant therapy
    • Nelson S.K., Bose S.K., Grunwald G.K., Myhill P., and McCord J.M. The induction of human superoxide dismutase and catalase in vivo: a fundamentally new approach to antioxidant therapy. Free Radic. Biol. Med. 40 (2006) 341-347
    • (2006) Free Radic. Biol. Med. , vol.40 , pp. 341-347
    • Nelson, S.K.1    Bose, S.K.2    Grunwald, G.K.3    Myhill, P.4    McCord, J.M.5
  • 289
    • 0002986799 scopus 로고
    • Is superoxide important in oxygen poisoning?
    • Fee J.A. Is superoxide important in oxygen poisoning?. Trends Biochem. Sci. 7 (1982) 84-86
    • (1982) Trends Biochem. Sci. , vol.7 , pp. 84-86
    • Fee, J.A.1


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