메뉴 건너뛰기




Volumn 287, Issue 17, 2012, Pages 13541-13548

Battles with iron: Manganese in oxidative stress protection

Author keywords

[No Author keywords available]

Indexed keywords

ANTIOXIDANT PROPERTIES; CELLULAR ADAPTATION; COFACTORS; FENTON CHEMISTRY; MANGANESE SUPEROXIDE DISMUTASE; OXIDATIVE DAMAGE; PROOXIDANT; REDOX-ACTIVE METALS; SIDE EFFECT;

EID: 84859976622     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.R111.312181     Document Type: Short Survey
Times cited : (235)

References (87)
  • 1
    • 44849094154 scopus 로고    scopus 로고
    • Diversity, function and evolution of genes coding for putative Ni-containing superoxide dismutases
    • DOI 10.1111/j.1462-2920.2008.01604.x
    • Dupont, C. L., Neupane, K., Shearer, J., and Palenik, B. (2008) Diversity, function, and evolution of genes coding for putative nickel-containing superoxide dismutases. Environ. Microbiol. 10, 1831-1843 (Pubitemid 351793623)
    • (2008) Environmental Microbiology , vol.10 , Issue.7 , pp. 1831-1843
    • Dupont, C.L.1    Neupane, K.2    Shearer, J.3    Palenik, B.4
  • 2
    • 0024978426 scopus 로고
    • Evolution and regulation of the gene encoding superoxide dismutase from the archaebacterium Halobacterium cutirubrum
    • May, B. P., and Dennis, P. P. (1989) Evolution and regulation of the gene encoding superoxide dismutase from the archaebacterium Halobacterium cutirubrum. J. Biol. Chem. 264, 12253-12258
    • (1989) J. Biol. Chem. , vol.264 , pp. 12253-12258
    • May, B.P.1    Dennis, P.P.2
  • 3
    • 1542305367 scopus 로고    scopus 로고
    • Specificity and phenetic relationships of iron- and manganese-containing superoxide dismutases on the basis of structure and sequence comparisons
    • Wintjens, R., Noël, C., May, A. C., Gerbod, D., Dufernez, F., Capron, M., Viscogliosi, E., and Rooman, M. (2004) Specificity and phenetic relationships of iron- and manganese-containing superoxide dismutases on the basis of structure and sequence comparisons. J. Biol. Chem. 279, 9248-9254
    • (2004) J. Biol. Chem. , vol.279 , pp. 9248-9254
    • Wintjens, R.1    Noël, C.2    May, A.C.3    Gerbod, D.4    Dufernez, F.5    Capron, M.6    Viscogliosi, E.7    Rooman, M.8
  • 4
    • 0348049820 scopus 로고    scopus 로고
    • The irony of manganese superoxide dismutase
    • Whittaker, J. W. (2003) The irony of manganese superoxide dismutase. Biochem. Soc. Trans. 31, 1318-1321
    • (2003) Biochem. Soc. Trans. , vol.31 , pp. 1318-1321
    • Whittaker, J.W.1
  • 6
    • 69949113909 scopus 로고    scopus 로고
    • The right to choose: Multiple pathways for activating copper,zinc superoxide dismutase
    • Leitch, J. M., Yick, P. J., and Culotta, V. C. (2009) The right to choose: multiple pathways for activating copper,zinc superoxide dismutase. J. Biol. Chem. 284, 24679-24683
    • (2009) J. Biol. Chem. , vol.284 , pp. 24679-24683
    • Leitch, J.M.1    Yick, P.J.2    Culotta, V.C.3
  • 7
    • 0035968001 scopus 로고    scopus 로고
    • Femtomolar sensitivity of metalloregulatory proteins controlling zinc homeostasis
    • DOI 10.1126/science.1060331
    • Outten, C. E., and O'Halloran, T. V. (2001) Femtomolar sensitivity of metalloregulatory proteins controlling zinc homeostasis. Science 292, 2488-2492 (Pubitemid 32605687)
    • (2001) Science , vol.292 , Issue.5526 , pp. 2488-2492
    • Outten, C.E.1    O'Halloran, T.V.2
  • 8
    • 77956892282 scopus 로고    scopus 로고
    • The effect of phosphate accumulation on metal ion homeostasis in Saccharomyces cerevisiae
    • Rosenfeld, L., Reddi, A. R., Leung, E., Aranda, K., Jensen, L. T., and Culotta, V. C. (2010) The effect of phosphate accumulation on metal ion homeostasis in Saccharomyces cerevisiae. J. Biol. Inorg. Chem. 15, 1051-1062
    • (2010) J. Biol. Inorg. Chem. , vol.15 , pp. 1051-1062
    • Rosenfeld, L.1    Reddi, A.R.2    Leung, E.3    Aranda, K.4    Jensen, L.T.5    Culotta, V.C.6
  • 9
    • 33644945987 scopus 로고    scopus 로고
    • Characterization of the yeast ionome: A genomewide analysis of nutrient mineral and trace element homeostasis in Saccharomyces cerevisiae
    • Eide, D. J., Clark, S., Nair, T. M., Gehl, M., Gribskov, M., Guerinot, M. L., and Harper, J. F. (2005) Characterization of the yeast ionome: a genomewide analysis of nutrient mineral and trace element homeostasis in Saccharomyces cerevisiae. Genome Biol. 6, R77
    • (2005) Genome Biol. , vol.6
    • Eide, D.J.1    Clark, S.2    Nair, T.M.3    Gehl, M.4    Gribskov, M.5    Guerinot, M.L.6    Harper, J.F.7
  • 10
    • 3042602322 scopus 로고    scopus 로고
    • Calometric studies on the tight binding metal interactions of Escherichia coli manganese superoxide dismutase
    • DOI 10.1074/jbc.M400813200
    • Mizuno, K., Whittaker, M. M., Bächinger, H. P., and Whittaker, J. W. (2004) Calorimetric studies on the tight-binding metal interactions of Escherichia coli manganese superoxide dismutase. J. Biol. Chem. 279, 27339-27344 (Pubitemid 38821020)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.26 , pp. 27339-27344
    • Mizuno, K.1    Whittaker, M.M.2    Bachinger, H.P.3    Whittaker, J.W.4
  • 11
    • 79953182648 scopus 로고    scopus 로고
    • Manganese complexes displaying superoxide dismutase activity: A balance between different factors
    • Iranzo, O. (2011) Manganese complexes displaying superoxide dismutase activity: a balance between different factors. Bioorg. Chem. 39, 73-87
    • (2011) Bioorg. Chem. , vol.39 , pp. 73-87
    • Iranzo, O.1
  • 13
    • 74449090930 scopus 로고    scopus 로고
    • Post-translational modifications of superoxide dismutase
    • Yamakura, F., and Kawasaki, H. (2010) Post-translational modifications of superoxide dismutase. Biochim. Biophys. Acta 1804, 318-325
    • (2010) Biochim. Biophys. Acta , vol.1804 , pp. 318-325
    • Yamakura, F.1    Kawasaki, H.2
  • 14
    • 34250879721 scopus 로고    scopus 로고
    • In vitro preparation of iron-substituted human manganese superoxide dismutase: Possible toxic properties for mitochondria
    • DOI 10.1016/j.freeradbiomed.2007.04.024, PII S0891584907002912
    • Yamakura, F., Kobayashi, K., Furukawa, S., and Suzuki, Y. (2007) In vitro preparation of iron-substituted human manganese superoxide dismutase: possible toxic properties for mitochondria. Free Radic. Biol. Med. 43, 423-430 (Pubitemid 46977630)
    • (2007) Free Radical Biology and Medicine , vol.43 , Issue.3 , pp. 423-430
    • Yamakura, F.1    Kobayashi, K.2    Furukawa, S.3    Suzuki, Y.4
  • 15
    • 0032573845 scopus 로고    scopus 로고
    • A simple proposal that can explain the inactivity of metal-substituted superoxide dismutases
    • DOI 10.1021/ja972060j
    • Vance, C. K., and Miller, A. F. (1998) A simple proposal that can explain the inactivity of metal-substituted superoxide dismutases. J. Am. Chem. Soc. 120, 461-467 (Pubitemid 28067812)
    • (1998) Journal of the American Chemical Society , vol.120 , Issue.3 , pp. 461-467
    • Vance, C.K.1    Miller, A.-F.2
  • 16
    • 3242706731 scopus 로고    scopus 로고
    • Combined spectroscopic/computational studies on iron- and manganese-dependent superoxide dismutases: Insights into second-sphere tuning of active site properties
    • Jackson, T. A., and Brunold, T. C. (2004) Combined spectroscopic/ computational studies on iron- and manganese-dependent superoxide dismutases: insights into second-sphere tuning of active site properties. Acc. Chem. Res. 37, 461-470
    • (2004) Acc. Chem. Res. , vol.37 , pp. 461-470
    • Jackson, T.A.1    Brunold, T.C.2
  • 17
    • 0026067789 scopus 로고
    • In vivo competition between iron and manganese for occupancy of the active site region of the manganese superoxide dismutase of Escherichia coli
    • Beyer, W. F., Jr., and Fridovich, I. (1991) In vivo competition between iron and manganese for occupancy of the active site region of the manganese superoxide dismutase of Escherichia coli. J. Biol. Chem. 266, 303-308
    • (1991) J. Biol. Chem. , vol.266 , pp. 303-308
    • Beyer Jr., W.F.1    Fridovich, I.2
  • 18
    • 0026794023 scopus 로고
    • Transcriptional and maturational effects of manganese and iron on the biosynthesis of manganese superoxide dismutase in Escherichia coli
    • Privalle, C. T., and Fridovich, I. (1992) Transcriptional and maturational effects of manganese and iron on the biosynthesis of manganese superoxide dismutase in Escherichia coli. J. Biol. Chem. 267, 9140-9145
    • (1992) J. Biol. Chem. , vol.267 , pp. 9140-9145
    • Privalle, C.T.1    Fridovich, I.2
  • 19
    • 0033521027 scopus 로고    scopus 로고
    • Thermally triggered metal binding by recombinant Thermus thermophilus manganese superoxide dismutase, expressed as the apo-enzyme
    • Whittaker, M. M., and Whittaker, J. W. (1999) Thermally triggered metal binding by recombinant Thermus thermophilus manganese superoxide dismutase, expressed as the apoenzyme. J. Biol. Chem. 274, 34751-34757 (Pubitemid 129509517)
    • (1999) Journal of Biological Chemistry , vol.274 , Issue.49 , pp. 34751-34757
    • Whittaker, M.M.1    Whittaker, J.W.2
  • 20
    • 0035941352 scopus 로고    scopus 로고
    • Candida albicans expresses an unusual cytoplasmic manganese-containing superoxide dismutase (SOD3 gene product) upon the entry and during the stationary phase
    • Lamarre, C., LeMay, J. D., Deslauriers, N., and Bourbonnais, Y. (2001) Candida albicans expresses an unusual cytoplasmic manganese-containing superoxide dismutase (SOD3 gene product) upon the entry and during the stationary phase. J. Biol. Chem. 276, 43784-43791
    • (2001) J. Biol. Chem. , vol.276 , pp. 43784-43791
    • Lamarre, C.1    LeMay, J.D.2    Deslauriers, N.3    Bourbonnais, Y.4
  • 21
    • 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, W. F., Jr., Hallewell, R. A., and Tainer, J. A. (1992) The structure of human mitochondrial manganese superoxide dismutase reveals a novel tetrameric interface of two 4-helix bundles. Cell 71, 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
  • 22
    • 80053229280 scopus 로고    scopus 로고
    • The superoxide dismutase SodA is targeted to the periplasm in a SecA-dependent manner by a novel mechanism
    • Krehenbrink, M., Edwards, A., and Downie, J. A. (2011) The superoxide dismutase SodA is targeted to the periplasm in a SecA-dependent manner by a novel mechanism. Mol. Microbiol. 82, 164-179
    • (2011) Mol. Microbiol. , vol.82 , pp. 164-179
    • Krehenbrink, M.1    Edwards, A.2    Downie, J.A.3
  • 23
    • 0035168223 scopus 로고    scopus 로고
    • Occurrence of two superoxide dismutases in Aeromonas hydrophila: Molecular cloning and differential expression of the sodA and sodB genes
    • Leclère, V., Chotteau-Lelièvre, A., Gancel, F., Imbert, M., and Blondeau, R. (2001) Occurrence of two superoxide dismutases in Aeromonas hydrophila: molecular cloning and differential expression of the sodA and sodB genes. Microbiology 147, 3105-3111 (Pubitemid 33076998)
    • (2001) Microbiology , vol.147 , Issue.11 , pp. 3105-3111
    • Leclere, V.1    Chotteau-Lelievre, A.2    Gancel, F.3    Imbert, M.4    Blondeau, R.5
  • 24
    • 0343487762 scopus 로고    scopus 로고
    • Nucleotide sequence of a putative periplasmic Mn superoxide dismutase from Acinetobacter calcoaceticus ADP1
    • DOI 10.1016/S0378-1119(96)00728-7, PII S0378111996007287
    • Geissdörfer, W., Ratajczak, A., and Hillen, W. (1997) Nucleotide sequence of a putative periplasmic manganese superoxide dismutase from Acinetobacter calcoaceticus ADP1. Gene 186, 305-308 (Pubitemid 27107700)
    • (1997) Gene , vol.186 , Issue.2 , pp. 305-308
    • Geissdorfer, W.1    Ratajczak, A.2    Hillen, W.3
  • 25
    • 37449030210 scopus 로고    scopus 로고
    • Multiple superoxide dismutases in Agrobacterium tumefaciens: Functional analysis, gene regulation, and influence on tumorigenesis
    • Saenkham, P., Eiamphungporn, W., Farrand, S. K., Vattanaviboon, P., and Mongkolsuk, S. (2007) Multiple superoxide dismutases in Agrobacterium tumefaciens: functional analysis, gene regulation, and influence on tumorigenesis. J. Bacteriol. 189, 8807-8817
    • (2007) J. Bacteriol. , vol.189 , pp. 8807-8817
    • Saenkham, P.1    Eiamphungporn, W.2    Farrand, S.K.3    Vattanaviboon, P.4    Mongkolsuk, S.5
  • 26
    • 0037673252 scopus 로고    scopus 로고
    • SecA2 functions in the secretion of superoxide dismutase A and in the virulence of Mycobacterium tuberculosis
    • DOI 10.1046/j.1365-2958.2003.03438.x
    • Braunstein, M., Espinosa, B. J., Chan, J., Belisle, J. T., and Jacobs, W. R., Jr. (2003) SecA2 functions in the secretion of superoxide dismutase A and in the virulence of Mycobacterium tuberculosis. Mol. Microbiol. 48, 453-464 (Pubitemid 36819081)
    • (2003) Molecular Microbiology , vol.48 , Issue.2 , pp. 453-464
    • Braunstein, M.1    Espinosa, B.J.2    Chan, J.3    Belisle, J.T.4    Jacobs Jr., W.R.5
  • 29
    • 33646155960 scopus 로고    scopus 로고
    • The effects of mitochondrial iron homeostasis on cofactor specificity of superoxide dismutase 2
    • Yang, M., Cobine, P. A., Molik, S., Naranuntarat, A., Lill, R., Winge, D. R., and Culotta, V. C. (2006) The effects of mitochondrial iron homeostasis on cofactor specificity of superoxide dismutase 2. EMBO J. 25, 1775-1783
    • (2006) EMBO J. , vol.25 , pp. 1775-1783
    • Yang, M.1    Cobine, P.A.2    Molik, S.3    Naranuntarat, A.4    Lill, R.5    Winge, D.R.6    Culotta, V.C.7
  • 30
    • 20744444389 scopus 로고    scopus 로고
    • Manganese activation of superoxide dismutase 2 in the mitochondria of Saccharomyces cerevisiae
    • DOI 10.1074/jbc.M504257200
    • Luk, E., Yang, M., Jensen, L. T., Bourbonnais, Y., and Culotta, V. C. (2005) Manganese activation of superoxide dismutase 2 in the mitochondria of Saccharomyces cerevisiae. J. Biol. Chem. 280, 22715-22720 (Pubitemid 40853176)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.24 , pp. 22715-22720
    • Luk, E.1    Yang, M.2    Jensen, L.T.3    Bourbonnais, Y.4    Culotta, V.C.5
  • 31
    • 78651238402 scopus 로고    scopus 로고
    • Subunit dissociation and metal binding by Escherichia coli apo-manganese superoxide dismutase
    • Whittaker, M. M., Lerch, T. F., Kirillova, O., Chapman, M. S., and Whittaker, J. W. (2011) Subunit dissociation and metal binding by Escherichia coli apo-manganese superoxide dismutase. Arch. Biochem. Biophys. 505, 213-225
    • (2011) Arch. Biochem. Biophys. , vol.505 , pp. 213-225
    • Whittaker, M.M.1    Lerch, T.F.2    Kirillova, O.3    Chapman, M.S.4    Whittaker, J.W.5
  • 32
    • 70350336540 scopus 로고    scopus 로고
    • In vitro metal uptake by recombinant human manganese superoxide dismutase
    • Whittaker, M. M., and Whittaker, J. W. (2009) In vitro metal uptake by recombinant human manganese superoxide dismutase. Arch. Biochem. Biophys. 491, 69-74
    • (2009) Arch. Biochem. Biophys. , vol.491 , pp. 69-74
    • Whittaker, M.M.1    Whittaker, J.W.2
  • 33
    • 33646183436 scopus 로고    scopus 로고
    • Kinetic analysis of the metal-binding mechanism of Escherichia coli manganese superoxide dismutase
    • Whittaker, M. M., Mizuno, K., Bächinger, H. P., and Whittaker, J. W. (2006) Kinetic analysis of the metal-binding mechanism of Escherichia coli manganese superoxide dismutase. Biophys. J. 90, 598-607
    • (2006) Biophys. J. , vol.90 , pp. 598-607
    • Whittaker, M.M.1    Mizuno, K.2    Bächinger, H.P.3    Whittaker, J.W.4
  • 35
    • 14744294785 scopus 로고    scopus 로고
    • Iron-sulfur protein biogenesis in eukaryotes
    • Lill, R., and Mühlenhoff, U. (2005) Iron-sulfur protein biogenesis in eukaryotes. Trends Biochem. Sci. 30, 133-141
    • (2005) Trends Biochem. Sci. , vol.30 , pp. 133-141
    • Lill, R.1    Mühlenhoff, U.2
  • 36
    • 17144378216 scopus 로고    scopus 로고
    • Iron-sulphur cluster biogenesis and mitochondrial iron homeostasis
    • DOI 10.1038/nrm1620
    • Rouault, T. A., and Tong, W. H. (2005) Iron-sulfur cluster biogenesis and mitochondrial iron homeostasis. Nat. Rev. Mol. Cell Biol. 6, 345-351 (Pubitemid 40516901)
    • (2005) Nature Reviews Molecular Cell Biology , vol.6 , Issue.4 , pp. 345-351
    • Rouault, T.A.1    Tong, W.-H.2
  • 38
    • 0034595617 scopus 로고    scopus 로고
    • Lack of a role for iron in the Lyme disease pathogen
    • DOI 10.1126/science.288.5471.1651
    • Posey, J. E., and Gherardini, F. C. (2000) Lack of a role for iron in the Lyme disease pathogen. Science 288, 1651-1653 (Pubitemid 30387432)
    • (2000) Science , vol.288 , Issue.5471 , pp. 1651-1653
    • Posey, J.E.1    Gherardini, F.C.2
  • 39
    • 0019475137 scopus 로고
    • Manganese and defenses against oxygen toxicity in Lactobacillus plantarum
    • Archibald, F. S., and Fridovich, I. (1981) Manganese and defenses against oxygen toxicity in Lactobacillus plantarum. J. Bacteriol. 145, 442-451 (Pubitemid 11140325)
    • (1981) Journal of Bacteriology , vol.145 , Issue.1 , pp. 442-451
    • Archibald, F.S.1    Fridovich, I.2
  • 40
    • 0034973791 scopus 로고    scopus 로고
    • Accumulation of manganese in Neisseria gonorrhoeae correlates with resistance to oxidative killing by superoxide anion and is independent of superoxide dismutase activity
    • DOI 10.1046/j.1365-2958.2001.02460.x
    • Tseng, H. J., Srikhanta, Y., McEwan, A. G., and Jennings, M. P. (2001) Accumulation of manganese in Neisseria gonorrhoeae correlates with resistance to oxidative killing by superoxide anion and is independent of superoxide dismutase activity. Mol. Microbiol. 40, 1175-1186 (Pubitemid 32574984)
    • (2001) Molecular Microbiology , vol.40 , Issue.5 , pp. 1175-1186
    • Tseng, H.-J.1    Srikhanta, Y.2    McEwan, A.G.3    Jennings, M.P.4
  • 41
    • 0036612888 scopus 로고    scopus 로고
    • Manganese supplementation relieves the phenotypic deficits seen in superoxide-dismutase-null Escherichia coli
    • DOI 10.1016/S0003-9861(02)00065-6, PII S0003986102000656
    • Al-Maghrebi, M., Fridovich, I., and Benov, L. (2002) Manganese supplementation relieves the phenotypic deficits seen in superoxide dismutasenull Escherichia coli. Arch. Biochem. Biophys. 402, 104-109 (Pubitemid 34848299)
    • (2002) Archives of Biochemistry and Biophysics , vol.402 , Issue.1 , pp. 104-109
    • Al-Maghrebi, M.1    Fridovich, I.2    Benov, L.3
  • 42
    • 0033037716 scopus 로고    scopus 로고
    • SodA and manganese are essential for resistance to oxidative stress in growing and sporulating cells of Bacillus subtilis
    • Inaoka, T., Matsumura, Y., and Tsuchido, T. (1999) SodA and manganese are essential for resistance to oxidative stress in growing and sporulating cells of Bacillus subtilis. J. Bacteriol. 181, 1939-1943 (Pubitemid 29138632)
    • (1999) Journal of Bacteriology , vol.181 , Issue.6 , pp. 1939-1943
    • Inaoka, T.1    Matsumura, Y.2    Tsuchido, T.3
  • 43
    • 0024391033 scopus 로고
    • Intracellular Mn(II)-associated superoxide scavenging activity protects Cu,Zn superoxide dismutase-deficient Saccharomyces cerevisiae against dioxygen stress
    • Chang, E. C., and Kosman, D. J. (1989) Intracellular Mn(II)-associated superoxide-scavenging activity protects Cu,Zn-superoxide dismutase-deficient Saccharomyces cerevisiae against dioxygen stress. J. Biol. Chem. 264, 12172-12178 (Pubitemid 19191100)
    • (1989) Journal of Biological Chemistry , vol.264 , Issue.21 , pp. 12172-12178
    • Chang, E.C.1    Kosman, D.J.2
  • 46
    • 0028134969 scopus 로고
    • The requirement for yeast superoxide dismutase is bypassed through mutations in BSD2, a novel metal homeostasis gene
    • Liu, X. F., and Culotta, V. C. (1994) The requirement for yeast superoxide dismutase is bypassed through mutations in BSD2, a novel metal homeostasis gene. Mol. Cell. Biol. 14, 7037-7045 (Pubitemid 24326367)
    • (1994) Molecular and Cellular Biology , vol.14 , Issue.11 , pp. 7037-7045
    • Liu, X.F.1    Culotta, V.C.2
  • 47
    • 0028889152 scopus 로고
    • Mutations in PMR1 suppress oxidative damage in yeast cells lacking superoxide dismutase
    • Lapinskas, P. J., Cunningham, K. W., Liu, X. F., Fink, G. R., and Culotta, V. C. (1995) Mutations in PMR1 suppress oxidative damage in yeast cells lacking superoxide dismutase. Mol. Cell. Biol. 15, 1382-1388
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 1382-1388
    • Lapinskas, P.J.1    Cunningham, K.W.2    Liu, X.F.3    Fink, G.R.4    Culotta, V.C.5
  • 48
    • 0029806025 scopus 로고    scopus 로고
    • Suppression of oxidative damage by Saccharomyces cerevisiae ATX2, which encodes a manganese-trafficking protein that localizes to Golgi-like vesicles
    • Lin, S. J., and Culotta, V. C. (1996) Suppression of oxidative damage by Saccharomyces cerevisiae ATX2, which encodes a manganese-trafficking protein that localizes to Golgi-like vesicles. Mol. Cell. Biol. 16, 6303-6312
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 6303-6312
    • Lin, S.J.1    Culotta, V.C.2
  • 49
    • 0001726322 scopus 로고    scopus 로고
    • Negative control of heavy metal uptake by the Saccharomyces cerevisiae BSD2 gene
    • DOI 10.1074/jbc.272.18.11763
    • Liu, X. F., Supek, F., Nelson, N., and Culotta, V. C. (1997) Negative control of heavy metal uptake by the Saccharomyces cerevisiae BSD2 gene. J. Biol. Chem. 272, 11763-11769 (Pubitemid 27202742)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.18 , pp. 11763-11769
    • Liu, X.F.1    Supek, F.2    Nelson, N.3    Culotta, V.C.4
  • 52
  • 54
    • 60749095652 scopus 로고    scopus 로고
    • A new perspective on radiation resistance based on Deinococcus radiodurans
    • Daly, M. J. (2009) A new perspective on radiation resistance based on Deinococcus radiodurans. Nat. Rev. Microbiol. 7, 237-245
    • (2009) Nat. Rev. Microbiol. , vol.7 , pp. 237-245
    • Daly, M.J.1
  • 55
    • 33745347750 scopus 로고    scopus 로고
    • Modulating radiation resistance: Insights based on defenses against reactive oxygen species in the radioresistant bacterium Deinococcus radiodurans
    • Daly, M. J. (2006) Modulating radiation resistance: insights based on defenses against reactive oxygen species in the radioresistant bacterium Deinococcus radiodurans. Clin. Lab. Med. 26, 491-504
    • (2006) Clin. Lab. Med. , vol.26 , pp. 491-504
    • Daly, M.J.1
  • 57
    • 12744273945 scopus 로고    scopus 로고
    • Caenorhabditis elegans PMR1, a P-type calcium ATPase, is important for calcium/manganese homeostasis and oxidative stress response
    • Cho, J. H., Ko, K. M., Singaravelu, G., and Ahnn, J. (2005) Caenorhabditis elegans PMR1, a P-type calcium ATPase, is important for calcium/manganese homeostasis and oxidative stress response. FEBS Lett. 579, 778-782
    • (2005) FEBS Lett. , vol.579 , pp. 778-782
    • Cho, J.H.1    Ko, K.M.2    Singaravelu, G.3    Ahnn, J.4
  • 58
    • 33644898819 scopus 로고    scopus 로고
    • Manganous ion supplementation accelerates wild-type development, enhances stress resistance, and rescues the life span of a short-lived Caenorhabditis elegans mutant
    • Lin, Y. T., Hoang, H., Hsieh, S. I., Rangel, N., Foster, A. L., Sampayo, J. N., Lithgow, G. J., and Srinivasan, C. (2006) Manganous ion supplementation accelerates wild-type development, enhances stress resistance, and rescues the life span of a short-lived Caenorhabditis elegans mutant. Free Radic. Biol. Med. 40, 1185-1193
    • (2006) Free Radic. Biol. Med. , vol.40 , pp. 1185-1193
    • Lin, Y.T.1    Hoang, H.2    Hsieh, S.I.3    Rangel, N.4    Foster, A.L.5    Sampayo, J.N.6    Lithgow, G.J.7    Srinivasan, C.8
  • 59
    • 0020464105 scopus 로고
    • Investigations of the state of manganese in Lactobacillus plantarum
    • DOI 10.1016/0003-9861(82)90120-5
    • Archibald, F. S., and Fridovich, I. (1982) Investigations of the state of the manganese in Lactobacillus plantarum. Arch. Biochem. Biophys. 215, 589-596 (Pubitemid 13189631)
    • (1982) Archives of Biochemistry and Biophysics , vol.215 , Issue.2 , pp. 589-596
    • Archibald, F.S.1    Fridovich, I.2
  • 61
    • 83455177151 scopus 로고    scopus 로고
    • Regulation of manganese antioxidants by nutrient-sensing pathways in Saccharomyces cerevisiae
    • Reddi, A. R., and Culotta, V. C. (2011) Regulation of manganese antioxidants by nutrient-sensing pathways in Saccharomyces cerevisiae. Genetics 189, 1261-1270
    • (2011) Genetics , vol.189 , pp. 1261-1270
    • Reddi, A.R.1    Culotta, V.C.2
  • 62
    • 0020118402 scopus 로고
    • The scavenging of superoxide radical by manganous complexes: In vitro
    • Archibald, F. S., and Fridovich, I. (1982) The scavenging of superoxide radical by manganous complexes: in vitro. Arch. Biochem. Biophys. 214, 452-463
    • (1982) Arch. Biochem. Biophys. , vol.214 , pp. 452-463
    • Archibald, F.S.1    Fridovich, I.2
  • 66
    • 0037901860 scopus 로고    scopus 로고
    • Genomic DNA of Nostoc commune (Cyanobacteria) becomes covalently modified during long-term (decades) desiccation but is protected from oxidative damage and degradation
    • DOI 10.1093/nar/gkg404
    • Shirkey, B., McMaster, N. J., Smith, S. C., Wright, D. J., Rodriguez, H., Jaruga, P., Birincioglu, M., Helm, R. F., and Potts, M. (2003) GenomicDNA of Nostoc commune (Cyanobacteria) becomes covalently modified during long-term (decades) desiccation but is protected from oxidative damage and degradation. Nucleic Acids Res. 31, 2995-3005 (Pubitemid 37441757)
    • (2003) Nucleic Acids Research , vol.31 , Issue.12 , pp. 2995-3005
    • Shirkey, B.1    McMaster, N.J.2    Smith, S.C.3    Wright, D.J.4    Rodriguez, H.5    Jaruga, P.6    Birincioglu, M.7    Helm, R.F.8    Potts, M.9
  • 67
    • 77954735594 scopus 로고    scopus 로고
    • Superoxide dismutase mimics: Chemistry, pharmacology, and therapeutic potential
    • Batinić-Haberle, I., Rebouças, J. S., and Spasojević, I. (2010) Superoxide dismutase mimics: chemistry, pharmacology, and therapeutic potential. Antioxid. Redox Signal. 13, 877-918
    • (2010) Antioxid. Redox Signal. , vol.13 , pp. 877-918
    • Batinić-Haberle, I.1    Rebouças, J.S.2    Spasojević, I.3
  • 68
    • 0025012990 scopus 로고
    • Manganese-dependent disproportionation of hydrogen peroxide in bicarbonate buffer
    • Stadtman, E. R., Berlett, B. S., and Chock, P. B. (1990) Manganese-dependent disproportionation of hydrogen peroxide in bicarbonate buffer. Proc. Natl. Acad. Sci. U.S.A. 87, 384-388
    • (1990) Proc. Natl. Acad. Sci. U.S.A. , vol.87 , pp. 384-388
    • Stadtman, E.R.1    Berlett, B.S.2    Chock, P.B.3
  • 69
    • 79953896180 scopus 로고    scopus 로고
    • Iron enzyme ribulose-5-phosphate 3-epimerase in Escherichia coli is rapidly damaged by hydrogen peroxide but can be protected by manganese
    • Sobota, J. M., and Imlay, J. A. (2011) Iron enzyme ribulose-5-phosphate 3-epimerase in Escherichia coli is rapidly damaged by hydrogen peroxide but can be protected by manganese. Proc. Natl. Acad. Sci. U.S.A. 108, 5402-5407
    • (2011) Proc. Natl. Acad. Sci. U.S.A. , vol.108 , pp. 5402-5407
    • Sobota, J.M.1    Imlay, J.A.2
  • 70
    • 65549107862 scopus 로고    scopus 로고
    • Manganese import is a key element of the OxyR response to hydrogen peroxide in Escherichia coli
    • Anjem, A., Varghese, S., and Imlay, J. A. (2009) Manganese import is a key element of the OxyR response to hydrogen peroxide in Escherichia coli. Mol. Microbiol. 72, 844-858
    • (2009) Mol. Microbiol. , vol.72 , pp. 844-858
    • Anjem, A.1    Varghese, S.2    Imlay, J.A.3
  • 71
    • 0036842345 scopus 로고    scopus 로고
    • Manganese: Elemental defence for a life with oxygen?
    • DOI 10.1016/S0966-842X(02)02462-9, PII S0966842X02024629
    • Horsburgh, M. J., Wharton, S. J., Karavolos, M., and Foster, S. J. (2002) Manganese: elemental defense for a life with oxygen. Trends Microbiol. 10, 496-501 (Pubitemid 35284795)
    • (2002) Trends in Microbiology , vol.10 , Issue.11 , pp. 496-501
    • Horsburgh, M.J.1    Wharton, S.J.2    Karavolos, M.3    Foster, S.J.4
  • 75
    • 66849111399 scopus 로고    scopus 로고
    • Gis1 is required for transcriptional reprogramming of carbon metabolism and the stress response during transition into stationary phase in yeast
    • Zhang, N., Wu, J., and Oliver, S. G. (2009) Gis1 is required for transcriptional reprogramming of carbon metabolism and the stress response during transition into stationary phase in yeast. Microbiology 155, 1690-1698
    • (2009) Microbiology , vol.155 , pp. 1690-1698
    • Zhang, N.1    Wu, J.2    Oliver, S.G.3
  • 76
    • 0038240674 scopus 로고    scopus 로고
    • Emerging themes in manganese transport, biochemistry and pathogenesis in bacteria
    • DOI 10.1016/S0168-6445(03)00052-4
    • Kehres, D. G., and Maguire, M. E. (2003) Emerging themes in manganese transport, biochemistry, and pathogenesis in bacteria. FEMS Microbiol. Rev. 27, 263-290 (Pubitemid 36694659)
    • (2003) FEMS Microbiology Reviews , vol.27 , Issue.2-3 , pp. 263-290
    • Kehres, D.G.1    Maguire, M.E.2
  • 77
    • 0030868591 scopus 로고    scopus 로고
    • Competence and virulence of Streptococcus pneumoniae: Adc and PsaA mutants exhibit a requirement for Zn and Mn resulting from inactivation of putative ABC metal permeases
    • Dintilhac, A., Alloing, G., Granadel, C., and Claverys, J. P. (1997) Competence and virulence of Streptococcus pneumoniae: Adc and PsaA mutants exhibit a requirement for zinc and manganese resulting from inactivation of putative ABC metal permeases. Mol. Microbiol. 25, 727-739 (Pubitemid 27394570)
    • (1997) Molecular Microbiology , vol.25 , Issue.4 , pp. 727-739
    • Dintilhac, A.1    Alloing, G.2    Granadel, C.3    Claverys, J.-P.4
  • 78
    • 62549151384 scopus 로고    scopus 로고
    • A manganese transporter, BB0219 (BmtA), is required for virulence by the Lyme disease spirochete, Borrelia burgdorferi
    • Ouyang, Z., He, M., Oman, T., Yang, X. F., and Norgard, M. V. (2009) A manganese transporter, BB0219 (BmtA), is required for virulence by the Lyme disease spirochete, Borrelia burgdorferi. Proc. Natl. Acad. Sci. U.S.A. 106, 3449-3454
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , pp. 3449-3454
    • Ouyang, Z.1    He, M.2    Oman, T.3    Yang, X.F.4    Norgard, M.V.5
  • 79
    • 79953728457 scopus 로고    scopus 로고
    • Yersinia pseudotuberculosis mntH functions in intracellular manganese accumulation, which is essential for virulence and survival in cells expressing functional Nramp1
    • Champion, O. L., Karlyshev, A., Cooper, I. A., Ford, D. C., Wren, B. W., Duffield, M., Oyston, P. C., and Titball, R. W. (2011) Yersinia pseudotuberculosis mntH functions in intracellular manganese accumulation, which is essential for virulence and survival in cells expressing functional Nramp1. Microbiology 157, 1115-1122
    • (2011) Microbiology , vol.157 , pp. 1115-1122
    • Champion, O.L.1    Karlyshev, A.2    Cooper, I.A.3    Ford, D.C.4    Wren, B.W.5    Duffield, M.6    Oyston, P.C.7    Titball, R.W.8
  • 81
    • 77949885386 scopus 로고    scopus 로고
    • Nutritional immunity beyond iron: A role for manganese and zinc
    • Kehl-Fie, T. E., and Skaar, E. P. (2010) Nutritional immunity beyond iron: a role for manganese and zinc. Curr. Opin. Chem. Biol. 14, 218-224
    • (2010) Curr. Opin. Chem. Biol. , vol.14 , pp. 218-224
    • Kehl-Fie, T.E.1    Skaar, E.P.2
  • 82
    • 0030017159 scopus 로고    scopus 로고
    • The Bcg/Ity/Lsh locus: Genetic transfer of resistance to infections in C57BL/6J mice transgenic for the Nramp1(Gly169) allele
    • Govoni, G., Vidal, S., Gauthier, S., Skamene, E., Malo, D., and Gros, P. (1996) The Bcg/Ity/Lsh locus: genetic transfer of resistance to infections in C57BL/6J mice transgenic for the Nramp1 Gly-169 allele. Infect. Immun. 64, 2923-2929 (Pubitemid 26256126)
    • (1996) Infection and Immunity , vol.64 , Issue.8 , pp. 2923-2929
    • Govoni, G.1    Vidal, S.2    Gauthier, S.3    Skamene, E.4    Malo, D.5    Gros, P.6
  • 83
    • 0031051831 scopus 로고    scopus 로고
    • Expression of the human NRAMP1 gene in professional primary phagocytes: Studies in blood cells and in HL-60 promyelocytic leukemia
    • Cellier, M., Shustik, C., Dalton, W., Rich, E., Hu, J., Malo, D., Schurr, E., and Gros, P. (1997) Expression of the human NRAMP1 gene in professional primary phagocytes: studies in blood cells and in HL-60 promyelocytic leukemia. J. Leukocyte Biol. 61, 96-105 (Pubitemid 27079472)
    • (1997) Journal of Leukocyte Biology , vol.61 , Issue.1 , pp. 96-105
    • Cellier, M.1    Shustik, C.2    Dalton, W.3    Rich, E.4    Hu, J.5    Malo, D.6    Schurr, E.7    Gros, P.8
  • 84
    • 0034613681 scopus 로고    scopus 로고
    • Natural resistance to intracellular infections: Natural resistance-associated macrophage protein 1 (Nramp1) functions as a pH-dependent manganese transporter at the phagosomal membrane
    • Jabado, N., Jankowski, A., Dougaparsad, S., Picard, V., Grinstein, S., and Gros, P. (2000) Natural resistance to intracellular infections: natural resistance-associated macrophage protein 1 (Nramp1) functions as a pH-dependent manganese transporter at the phagosomal membrane. J. Exp. Med. 192, 1237-1248
    • (2000) J. Exp. Med. , vol.192 , pp. 1237-1248
    • Jabado, N.1    Jankowski, A.2    Dougaparsad, S.3    Picard, V.4    Grinstein, S.5    Gros, P.6
  • 86
    • 80051898476 scopus 로고    scopus 로고
    • Nutrient metal sequestration by calprotectin inhibits bacterial superoxide defense, enhancing neutrophil killing of Staphylococcus aureus
    • Kehl-Fie, T. E., Chitayat, S., Hood, M. I., Damo, S., Restrepo, N., Garcia, C., Munro, K. A., Chazin, W. J., and Skaar, E. P. (2011) Nutrient metal sequestration by calprotectin inhibits bacterial superoxide defense, enhancing neutrophil killing of Staphylococcus aureus. Cell Host Microbe 10, 158-164
    • (2011) Cell Host Microbe , vol.10 , pp. 158-164
    • Kehl-Fie, T.E.1    Chitayat, S.2    Hood, M.I.3    Damo, S.4    Restrepo, N.5    Garcia, C.6    Munro, K.A.7    Chazin, W.J.8    Skaar, E.P.9
  • 87
    • 77952674667 scopus 로고    scopus 로고
    • Mechanism of the peroxidase activity of Cu,Zn-superoxide dismutase
    • Liochev, S. I., and Fridovich, I. (2010) Mechanism of the peroxidase activity of Cu,Zn-superoxide dismutase. Free Radic. Biol. Med. 48, 1565-1569
    • (2010) Free Radic. Biol. Med. , vol.48 , pp. 1565-1569
    • Liochev, S.I.1    Fridovich, I.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.