메뉴 건너뛰기




Volumn 50, Issue 46, 2011, Pages 9940-9949

Bacterial transition metal P 1B-ATPases: Transport mechanism and roles in virulence

Author keywords

[No Author keywords available]

Indexed keywords

ATP BINDING; ATPASES; BACTERIAL GENOMES; CHELATING MOLECULES; CYTOPLASMIC DOMAINS; METAL BINDING; METAL BINDING DOMAIN; METAL EXCHANGE; METAL LEVELS; METALLO-PROTEINS; P-TYPE; PHYSIOLOGICAL FUNCTIONS; POLYTOPIC MEMBRANE PROTEINS; RECENT PROGRESS; STRUCTURAL SIMILARITY; TRANSMEMBRANE SEGMENTS; TRANSPORT MECHANISM;

EID: 81255142801     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi201418k     Document Type: Review
Times cited : (94)

References (103)
  • 2
    • 26444500150 scopus 로고    scopus 로고
    • Metalloproteomics: High-throughput structural and functional annotation of proteins in structural genomics
    • DOI 10.1016/j.str.2005.07.014, PII S0969212605002765
    • Shi, W., Zhan, C., Ignatov, A., Manjasetty, B. A., Marinkovic, N., Sullivan, M., Huang, R., and Chance, M. R. (2005) Metalloproteomics: high-throughput structural and functional annotation of proteins in structural genomics Structure 13, 1473-1486 (Pubitemid 41427587)
    • (2005) Structure , vol.13 , Issue.10 , pp. 1473-1486
    • Shi, W.1    Zhan, C.2    Ignatov, A.3    Manjasetty, B.A.4    Marinkovic, N.5    Sullivan, M.6    Huang, R.7    Chance, M.R.8
  • 4
    • 66249112833 scopus 로고    scopus 로고
    • The iron-sulfur clusters of dehydratases are primary intracellular targets of copper toxicity
    • Macomber, L. and Imlay, J. A. (2009) The iron-sulfur clusters of dehydratases are primary intracellular targets of copper toxicity Proc. Natl. Acad. Sci. U. S. A. 106, 8344-8349
    • (2009) Proc. Natl. Acad. Sci. U. S. A. , vol.106 , pp. 8344-8349
    • MacOmber, L.1    Imlay, J.A.2
  • 6
    • 0037565061 scopus 로고    scopus 로고
    • Efflux-mediated heavy metal resistance in prokaryotes
    • DOI 10.1016/S0168-6445(03)00048-2
    • Nies, D. H. (2003) Efflux-mediated heavy metal resistance in prokaryotes FEMS Microbiol. Rev. 27, 313-339 (Pubitemid 36700434)
    • (2003) FEMS Microbiology Reviews , vol.27 , Issue.2-3 , pp. 313-339
    • Nies, D.H.1
  • 7
    • 0035421993 scopus 로고    scopus 로고
    • Divalent-metal transport by NRAMP proteins at the interface of host-pathogen interactions
    • DOI 10.1016/S0966-842X(01)02098-4, PII S0966842X01020984
    • Forbes, J. R. and Gros, P. (2001) Divalent-metal transport by NRAMP proteins at the interface of host-pathogen interactions Trends Microbiol. 9, 397-403 (Pubitemid 32763067)
    • (2001) Trends in Microbiology , vol.9 , Issue.8 , pp. 397-403
    • Forbes, J.R.1    Gros, P.2
  • 9
    • 37249043376 scopus 로고    scopus 로고
    • The structural basis of calcium transport by the calcium pump
    • DOI 10.1038/nature06418, PII NATURE06418
    • Olesen, C., Picard, M., Winther, A. M., Gyrup, C., Morth, J. P., Oxvig, C., Moller, J. V., and Nissen, P. (2007) The structural basis of calcium transport by the calcium pump Nature 450, 1036-1042 (Pubitemid 350273617)
    • (2007) Nature , vol.450 , Issue.7172 , pp. 1036-1042
    • Olesen, C.1    Picard, M.2    Winther, A.-M.L.3    Gyrup, C.4    Morth, J.P.5    Oxvig, C.6    Moller, J.V.7    Nissen, P.8
  • 10
    • 0035997378 scopus 로고    scopus 로고
    • Biochemistry of Na,K-ATPase
    • DOI 10.1146/annurev.biochem.71.102201.141218
    • Kaplan, J. H. (2002) Biochemistry of Na,K-ATPase Annu. Rev. Biochem. 71, 511-535 (Pubitemid 34800229)
    • (2002) Annual Review of Biochemistry , vol.71 , pp. 511-535
    • Kaplan, J.H.1
  • 12
    • 34248633103 scopus 로고    scopus 로고
    • 1B- ATPases
    • DOI 10.1007/s10534-006-9055-6, Biometals: function and transport in bacteria, fungi, and humans
    • 1B-ATPases Biometals 20, 233-248 (Pubitemid 46776570)
    • (2007) BioMetals , vol.20 , Issue.3-4 , pp. 233-248
    • Arguello, J.M.1    Eren, E.2    Gonzalez-Guerrero, M.3
  • 14
    • 77953503319 scopus 로고    scopus 로고
    • CtpA, a copper-translocating P-type ATPase involved in the biogenesis of multiple copper-requiring enzymes
    • Hassani, B. K., Astier, C., Nitschke, W., and Ouchane, S. (2010) CtpA, a copper-translocating P-type ATPase involved in the biogenesis of multiple copper-requiring enzymes J. Biol. Chem. 285, 19330-19337
    • (2010) J. Biol. Chem. , vol.285 , pp. 19330-19337
    • Hassani, B.K.1    Astier, C.2    Nitschke, W.3    Ouchane, S.4
  • 15
    • 0029967233 scopus 로고    scopus 로고
    • 3-type cytochrome oxidase
    • DOI 10.1007/s002030050330
    • Preisig, O., Zufferey, R., and Hennecke, H. (1996) The Bradyrhizobium japonicum fixGHIS genes are required for the formation of the high-affinity cbb(3)-type cytochrome oxidase Arch. Microbiol. 165, 297-305 (Pubitemid 26175058)
    • (1996) Archives of Microbiology , vol.165 , Issue.5 , pp. 297-305
    • Preisig, O.1    Zufferey, R.2    Hennecke, H.3
  • 16
    • 0034677662 scopus 로고    scopus 로고
    • Roles of the ccoGHIS gene products in the biogenesis of the cbb(3)-type cytochrome c oxidase
    • Koch, H. G., Winterstein, C., Saribas, A. S., Alben, J. O., and Daldal, F. (2000) Roles of the ccoGHIS gene products in the biogenesis of the cbb(3)-type cytochrome c oxidase J. Mol. Biol. 297, 49-65
    • (2000) J. Mol. Biol. , vol.297 , pp. 49-65
    • Koch, H.G.1    Winterstein, C.2    Saribas, A.S.3    Alben, J.O.4    Daldal, F.5
  • 17
    • 22544432254 scopus 로고    scopus 로고
    • Mutations in the cueA gene encoding a copper homeostasis P-type ATPase reduce the pathogenicity of Pseudomonas aeruginosa in mice
    • DOI 10.1016/j.ijmm.2005.05.005, PII S1438422105000743
    • Schwan, W. R., Warrener, P., Keunz, E., Stover, C. K., and Folger, K. R. (2005) Mutations in the cueA gene encoding a copper homeostasis P-type ATPase reduce the pathogenicity of Pseudomonas aeruginosa in mice Int. J. Med. Microbiol. 295, 237-242 (Pubitemid 41020797)
    • (2005) International Journal of Medical Microbiology , vol.295 , Issue.4 , pp. 237-242
    • Schwan, W.R.1    Warrener, P.2    Keunz, E.3    Kendall Stover, C.4    Folger, K.R.5
  • 19
    • 0031964372 scopus 로고    scopus 로고
    • Evolution of substrate specificities in the P-type ATPase superfamily
    • DOI 10.1007/PL00006286
    • Axelsen, K. B. and Palmgren, M. G. (1998) Evolution of substrate specificities in the P-type ATPase superfamily J. Mol. Evol. 46, 84-101 (Pubitemid 28047242)
    • (1998) Journal of Molecular Evolution , vol.46 , Issue.1 , pp. 84-101
    • Axelsen, K.B.1    Palmgren, M.G.2
  • 20
    • 34447510930 scopus 로고    scopus 로고
    • Function and regulation of human copper-transporting ATPases
    • DOI 10.1152/physrev.00004.2006
    • Lutsenko, S., Barnes, N. L., Bartee, M. Y., and Dmitriev, O. Y. (2007) Function and regulation of human copper-transporting ATPases Physiol. Rev. 87, 1011-1046 (Pubitemid 47084675)
    • (2007) Physiological Reviews , vol.87 , Issue.3 , pp. 1011-1046
    • Lutsenko, S.1    Barnes, N.L.2    Bartee, M.Y.3    Dmitriev, O.Y.4
  • 21
    • 25844489990 scopus 로고    scopus 로고
    • 1B-ATPases - An ancient family of transition metal pumps with diverse functions in plants
    • DOI 10.1016/j.tplants.2005.08.008, PII S1360138505002050
    • 1B-ATPases - an ancient family of transition metal pumps with diverse functions in plants Trends Plant Sci. 10, 491-502 (Pubitemid 41395271)
    • (2005) Trends in Plant Science , vol.10 , Issue.10 , pp. 491-502
    • Williams, L.E.1    Mills, R.F.2
  • 22
    • 33544471308 scopus 로고    scopus 로고
    • Metal ion transport and regulation in Mycobacterium tuberculosis
    • Agranoff, D. and Krishna, S. (2004) Metal ion transport and regulation in Mycobacterium tuberculosis Front. Biosci. 9, 2996-3006
    • (2004) Front. Biosci. , vol.9 , pp. 2996-3006
    • Agranoff, D.1    Krishna, S.2
  • 28
    • 33947658924 scopus 로고    scopus 로고
    • Conservative and nonconservative mutations of the transmembrane CPC motif in ZntA: Effect on metal selectivity and activity
    • DOI 10.1021/bi0616394
    • Dutta, S. J., Liu, J., Stemmler, A. J., and Mitra, B. (2007) Conservative and nonconservative mutations of the transmembrane CPC motif in ZntA: effect on metal selectivity and activity Biochemistry 46, 3692-3703 (Pubitemid 46493470)
    • (2007) Biochemistry , vol.46 , Issue.12 , pp. 3692-3703
    • Dutta, S.J.1    Liu, J.2    Stemmler, A.J.3    Mitra, B.4
  • 29
    • 33750601861 scopus 로고    scopus 로고
    • 714 in the seventh and eighth transmembrane segments of ZntA contribute to the coupling of metal binding and ATPase activity
    • DOI 10.1016/j.bbabio.2006.06.008, PII S0005272806002106
    • Okkeri, J. and Haltia, T. (2006) The metal-binding sites of the zinc-transporting P-type ATPase of Escherichia coli. Lys693 and Asp714 in the seventh and eighth transmembrane segments of ZntA contribute to the coupling of metal binding and ATPase activity Biochim. Biophys. Acta 1757, 1485-1495 (Pubitemid 44679749)
    • (2006) Biochimica et Biophysica Acta - Bioenergetics , vol.1757 , Issue.11 , pp. 1485-1495
    • Okkeri, J.1    Haltia, T.2
  • 31
    • 44649182134 scopus 로고    scopus 로고
    • Structure of a Copper Pump Suggests a Regulatory Role for Its Metal-Binding Domain
    • DOI 10.1016/j.str.2008.02.025, PII S0969212608001512
    • Wu, C. C., Rice, W. J., and Stokes, D. L. (2008) Structure of a copper pump suggests a regulatory role for its metal-binding domain Structure 16, 976-985 (Pubitemid 351778383)
    • (2008) Structure , vol.16 , Issue.6 , pp. 976-985
    • Wu, C.-C.1    Rice, W.J.2    Stokes, D.L.3
  • 34
    • 0035910261 scopus 로고    scopus 로고
    • 1325 fragment of the Wilson's disease protein binds nucleotides and interacts with the N-terminal domain of this protein in a copper-dependent manner
    • DOI 10.1074/jbc.M003238200
    • Tsivkovskii, R., MacArthurs, B., and Lutsenko, S. (2001) The Lys(1010)-Lys(1325) fragment of the Wilson's disease protein binds nucleotides and interacts with the N-terminal domain of this protein in a copper-dependent manner J. Biol. Chem. 276, 2234-2242 (Pubitemid 32109707)
    • (2001) Journal of Biological Chemistry , vol.276 , Issue.3 , pp. 2234-2242
    • Tsivkovskii, R.1    MacArthur, B.C.2    Lutsenko, S.3
  • 35
    • 0141431021 scopus 로고    scopus 로고
    • +-ATPase CopA
    • DOI 10.1021/bi034806y
    • +-ATPase CopA Biochemistry 42, 11040-11047 (Pubitemid 37174396)
    • (2003) Biochemistry , vol.42 , Issue.37 , pp. 11040-11047
    • Mandal, A.K.1    Arguello, J.M.2
  • 37
    • 70350627430 scopus 로고    scopus 로고
    • Structural biology of copper trafficking
    • Boal, A. K. and Rosenzweig, A. C. (2009) Structural biology of copper trafficking Chem. Rev. 109, 4760-4779
    • (2009) Chem. Rev. , vol.109 , pp. 4760-4779
    • Boal, A.K.1    Rosenzweig, A.C.2
  • 38
    • 0036175362 scopus 로고    scopus 로고
    • Metallochaperones and metal-transporting ATPases: A comparative analysis of sequences and structures
    • DOI 10.1101/gr.196802
    • Arnesano, F., Banci, L., Bertini, I., Ciofi-Baffoni, S., Molteni, E., Huffman, D. L., and O'Halloran, T. V. (2002) Metallochaperones and metal-transporting ATPases: a comparative analysis of sequences and structures Genome Res. 12, 255-271 (Pubitemid 34162992)
    • (2002) Genome Research , vol.12 , Issue.2 , pp. 255-271
    • Arnesano, F.1    Banci, L.2    Bertini, I.3    Ciofi-Baffoni, S.4    Molteni, E.5    Huffman, D.L.6    O'Halloran, T.V.7
  • 40
    • 0034595406 scopus 로고    scopus 로고
    • A hemerythrin-like domain in a bacterial chemotaxis protein
    • DOI 10.1021/bi992796o
    • Xiong, J., Kurtz, D. M., Jr., Ai, J., and Sanders-Loehr, J. (2000) A hemerythrin-like domain in a bacterial chemotaxis protein Biochemistry 39, 5117-5125 (Pubitemid 30241634)
    • (2000) Biochemistry , vol.39 , Issue.17 , pp. 5117-5125
    • Xiong, J.1    Kurtz Jr., D.M.2    Ai, J.3    Sanders-Loehr, J.4
  • 42
    • 0037033056 scopus 로고    scopus 로고
    • Biochemical characterization of CopA, the Escherichia coli Cu(I)-translocating P-type ATPase
    • DOI 10.1074/jbc.M208490200
    • Fan, B. and Rosen, B. P. (2002) Biochemical characterization of CopA, the Escherichia coli Cu(I)- translocating P-type ATPase J. Biol. Chem. 277, 46987-46992 (Pubitemid 36159204)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.49 , pp. 46987-46992
    • Fan, B.1    Rosen, B.P.2
  • 43
    • 0037993832 scopus 로고    scopus 로고
    • Transition metal speciation in the cell: Insights from the chemistry of metal ion receptors
    • DOI 10.1126/science.1085049
    • Finney, L. A. and O'Halloran, T. V. (2003) Transition metal speciation in the cell: Insights from the chemistry of metal ion receptors Science 300, 931-936 (Pubitemid 36548870)
    • (2003) Science , vol.300 , Issue.5621 , pp. 931-936
    • Finney, L.A.1    O'Halloran, T.V.2
  • 44
    • 0034635468 scopus 로고    scopus 로고
    • The ATP hydrolytic activity of purified ZntA, a Pb(II)/Cd(II)/Zn(II)- translocating ATPase from Escherichia coli
    • DOI 10.1074/jbc.275.6.3873
    • Sharma, R., Rensing, C., Rosen, B. P., and Mitra, B. (2000) The ATP hydrolytic activity of purified ZntA, a Pb(II)/Cd(II)/Zn(II)-translocating ATPase from Escherichia coli J. Biol. Chem. 275, 3873-3878 (Pubitemid 30094611)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.6 , pp. 3873-3878
    • Sharma, R.1    Rensing, C.2    Rosen, B.P.3    Mitra, B.4
  • 46
    • 79960695783 scopus 로고    scopus 로고
    • The lumenal loop Met672-Pro707 of copper-transporting ATPase ATP7A binds metals and facilitates copper release from the intramembrane sites
    • Barry, A. N., Otoikhian, A., Bhatt, S., Shinde, U., Tsivkovskii, R., Blackburn, N. J., and Lutsenko, S. (2011) The lumenal loop Met672-Pro707 of copper-transporting ATPase ATP7A binds metals and facilitates copper release from the intramembrane sites J. Biol. Chem. 286, 26585-26594
    • (2011) J. Biol. Chem. , vol.286 , pp. 26585-26594
    • Barry, A.N.1    Otoikhian, A.2    Bhatt, S.3    Shinde, U.4    Tsivkovskii, R.5    Blackburn, N.J.6    Lutsenko, S.7
  • 47
    • 0035954407 scopus 로고    scopus 로고
    • The cysteine-rich amino-terminal domain of ZntA, a Pb(II)/Zn(II)/Cd(II)- translocating ATPase from Escherichia coli, is not essential for its function
    • Mitra, B. and Sharma, R. (2001) The cysteine-rich amino-terminal domain of ZntA, a Pb(II)/Zn(II)/Cd(II)-translocating ATPase from Escherichia coli, is not essential for its function Biochemistry 40, 7694-7699 (Pubitemid 32578033)
    • (2001) Biochemistry , vol.40 , Issue.25 , pp. 7694-7699
    • Mitra, B.1    Sharma, R.2
  • 48
    • 0142103656 scopus 로고    scopus 로고
    • 2+-ATPase: Functional role of its histidine-rich N-terminal metal binding domain
    • DOI 10.1074/jbc.M306907200
    • 2+-ATPase-Functional role of its histidine-rich N-terminal metal binding domain J. Biol. Chem. 278, 40534-40541 (Pubitemid 37280864)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.42 , pp. 40534-40541
    • Mana-Capelli, S.1    Mandal, A.K.2    Arguello, J.M.3
  • 49
    • 0037008692 scopus 로고    scopus 로고
    • 2-terminal domain of the Wilson's disease protein and regulates its catalytic activity
    • DOI 10.1074/jbc.M203845200
    • 2-terminal domain of the Wilson's disease protein and regulates its catalytic activity J. Biol. Chem. 277, 27953-27959 (Pubitemid 34966743)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.31 , pp. 27953-27959
    • Walker, J.M.1    Tsivkovskii, R.2    Lutsenko, S.3
  • 50
    • 0034705616 scopus 로고    scopus 로고
    • Energetics of copper trafficking between the Atx1 metallochaperone and the intracellular copper transporter, Ccc2
    • DOI 10.1074/jbc.C000172200
    • Huffman, D. L. and O'Halloran, T. V. (2000) Energetics of copper trafficking between the Atx1 metallochaperone and the intracellular copper transporter, Ccc2 J. Biol. Chem. 275, 18611-18614 (Pubitemid 30422815)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.25 , pp. 18611-18614
    • Huffman, D.L.1    O'Halloran, T.V.2
  • 51
    • 0027288228 scopus 로고
    • Primary structure of two P-type ATPases involved in copper homeostasis in Enterococcus hirae
    • Odermatt, A., Suter, H., Krapf, R., and Solioz, M. (1993) Primary structure of two P-type ATPases involved in copper homeostasis in Enterococcus hirae J. Biol. Chem. 268, 12775-12779 (Pubitemid 23182446)
    • (1993) Journal of Biological Chemistry , vol.268 , Issue.17 , pp. 12775-12779
    • Odermatt, A.1    Suter, H.2    Krapf, R.3    Solioz, M.4
  • 52
    • 0035827547 scopus 로고    scopus 로고
    • Two Menkes-type ATPases supply copper for photosynthesis in Synechocystis PCC 6803
    • Tottey, S., Rich, P. R., Rondet, S. A. M., and Robinson, N. J. (2001) Two Menkes-type ATPases supply copper for photosynthesis in Synechocystis PCC 6803 J. Biol. Chem. 276, 19999-20004
    • (2001) J. Biol. Chem. , vol.276 , pp. 19999-20004
    • Tottey, S.1    Rich, P.R.2    Rondet, S.A.M.3    Robinson, N.J.4
  • 53
  • 57
    • 0042208193 scopus 로고    scopus 로고
    • The metal specificity and selectivity of ZntA from Escherichia coli using the acylphosphate intermediate
    • DOI 10.1074/jbc.M301415200
    • Hou, Z. and Mitra, B. (2003) The metal specificity and selectivity of ZntA from Escherichia coli using the acylphosphate intermediate J. Biol. Chem. 278, 28455-28461 (Pubitemid 36935747)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.31 , pp. 28455-28461
    • Hou, Z.1    Mitra, B.2
  • 58
    • 31044446123 scopus 로고    scopus 로고
    • Metal-binding affinity of the transmembrane site in ZntA: Implications for metal selectivity
    • DOI 10.1021/bi051836n
    • Liu, J., Dutta, S. J., Stemmler, A. J., and Mitra, B. (2006) Metal-binding affinity of the transmembrane site in ZntA: implications for metal selectivity Biochemistry 45, 763-772 (Pubitemid 43122241)
    • (2006) Biochemistry , vol.45 , Issue.3 , pp. 763-772
    • Liu, J.1    Dutta, S.J.2    Stemmler, A.J.3    Mitra, B.4
  • 59
    • 70350637580 scopus 로고    scopus 로고
    • Coordination chemistry of bacterial metal transport and sensing
    • Ma, Z., Jacobsen, F. E., and Giedroc, D. P. (2009) Coordination chemistry of bacterial metal transport and sensing Chem. Rev. 109, 4644-4681
    • (2009) Chem. Rev. , vol.109 , pp. 4644-4681
    • Ma, Z.1    Jacobsen, F.E.2    Giedroc, D.P.3
  • 60
    • 0033520471 scopus 로고    scopus 로고
    • Cobalt-dependent transcriptional switching by a dual-effector MerR-like protein regulates a cobalt-exporting variant CPx-type ATPase
    • Rutherford, J. C., Cavet, J. S., and Robinson, N. J. (1999) Cobalt-dependent transcriptional switching by a dual-effector MerR-like protein regulates a cobalt-exporting variant CPx-type ATPase J. Biol. Chem. 274, 25827-25832
    • (1999) J. Biol. Chem. , vol.274 , pp. 25827-25832
    • Rutherford, J.C.1    Cavet, J.S.2    Robinson, N.J.3
  • 61
    • 70350146566 scopus 로고    scopus 로고
    • CzcP is a novel efflux system contributing to transition metal resistance in Cupriavidus metallidurans CH34
    • Scherer, J. and Nies, D. H. (2009) CzcP is a novel efflux system contributing to transition metal resistance in Cupriavidus metallidurans CH34 Mol. Microbiol. 73, 601-621
    • (2009) Mol. Microbiol. , vol.73 , pp. 601-621
    • Scherer, J.1    Nies, D.H.2
  • 62
    • 0025069608 scopus 로고
    • Zinc deficiency and immune function
    • Keen, C. L. and Gershwin, M. E. (1990) Zinc deficiency and immune function Annu. Rev. Nutr. 10, 415-431 (Pubitemid 120034155)
    • (1990) Annual Review of Nutrition , vol.10 , Issue.1 , pp. 415-431
    • Keen, C.L.1    Gershwin, M.E.2
  • 64
    • 0042871288 scopus 로고    scopus 로고
    • Iron deficiency and in vitro iron chelation reduce the expression of cluster of differentiation molecule (CD)28 but not CD3 receptors on murine thymocytes and spleen cells
    • DOI 10.1079/BJN2003864
    • Kuvibidila, S. R. and Porretta, C. (2003) Iron deficiency and in vitro iron chelation reduce the expression of cluster of differentiation molecule (CD)28 but not CD3 receptors on murine thymocytes and spleen cells Br. J. Nutr. 90, 179-189 (Pubitemid 36903416)
    • (2003) British Journal of Nutrition , vol.90 , Issue.1 , pp. 179-189
    • Kuvibidila, S.R.1    Porretta, C.2
  • 65
    • 0033822221 scopus 로고    scopus 로고
    • Effects of zinc deficiency on Th1 and Th2 cytokine shifts
    • Prasad, A. S. (2000) Effects of zinc deficiency on Th1 and Th2 cytokine shifts J. Infect. Dis. 182, S62-S68
    • (2000) J. Infect. Dis. , vol.182
    • Prasad, A.S.1
  • 67
    • 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
  • 68
    • 2342510407 scopus 로고    scopus 로고
    • IL-6 mediates hypoferremia of inflammation by inducing the synthesis of the iron regulatory hormone hepcidin
    • DOI 10.1172/JCI200420945
    • Nemeth, E., Rivera, S., Gabayan, V., Keller, C., Taudorf, S., Pedersen, B. K., and Ganz, T. (2004) IL-6 mediates hypoferremia of inflammation by inducing the synthesis of the iron regulatory hormone hepcidin J. Clin. Invest. 113, 1271-1276 (Pubitemid 39069926)
    • (2004) Journal of Clinical Investigation , vol.113 , Issue.9 , pp. 1271-1276
    • Nemeth, E.1    Rivera, S.2    Gabayan, V.3    Keller, C.4    Taudorf, S.5    Pedersen, B.K.6    Ganz, T.7
  • 70
    • 0028822588 scopus 로고
    • Calprotectin-mediated zinc chelation as a biostatic mechanism in host defence
    • Clohessy, P. A. and Golden, B. E. (1995) Calprotectin-mediated zinc chelation as a biostatic mechanism in host defence Scand. J. Immunol. 42, 551-556
    • (1995) Scand. J. Immunol. , vol.42 , pp. 551-556
    • Clohessy, P.A.1    Golden, B.E.2
  • 71
    • 28444462150 scopus 로고    scopus 로고
    • Lactoferrin: A modulator of immune and inflammatory responses
    • DOI 10.1007/s00018-005-5370-2
    • Legrand, D., Elass, E., Carpentier, M., and Mazurier, J. (2005) Lactoferrin: a modulator of immune and inflammatory responses Cell. Mol. Life Sci. 62, 2549-2559 (Pubitemid 41722207)
    • (2005) Cellular and Molecular Life Sciences , vol.62 , Issue.22 , pp. 2549-2559
    • Legrand, D.1    Elass, E.2    Carpentier, M.3    Mazurier, J.4
  • 74
    • 35448938485 scopus 로고    scopus 로고
    • Association of hemochromatosis with infectious diseases: expanding spectrum
    • DOI 10.1016/j.ijid.2007.04.007, PII S1201971207000811
    • Khan, F. A., Fisher, M. A., and Khakoo, R. A. (2007) Association of hemochromatosis with infectious diseases: expanding spectrum Int. J. Infect. Dis. 11, 482-487 (Pubitemid 47626050)
    • (2007) International Journal of Infectious Diseases , vol.11 , Issue.6 , pp. 482-487
    • Khan, F.A.1    Fisher, M.A.2    Khakoo, R.A.3
  • 75
    • 0003915574 scopus 로고    scopus 로고
    • 3 rd ed. Garland Science, New York.
    • Parham, P. (2009) The Immune System, 3 rd ed., Garland Science, New York.
    • (2009) The Immune System
    • Parham, P.1
  • 76
    • 77953646681 scopus 로고    scopus 로고
    • Oxidative burst and plant disease resistance
    • Averyanov, A. (2009) Oxidative burst and plant disease resistance Front. Biosci. 1, 142-152
    • (2009) Front. Biosci. , vol.1 , pp. 142-152
    • Averyanov, A.1
  • 77
    • 33645849237 scopus 로고    scopus 로고
    • Structures of the high-valent metal-ion haem-oxygen intermediates in peroxidases, oxygenases and catalases
    • Hersleth, H.-P., Ryde, U., Rydberg, P., Görbitz, C. H., and Andersson, K. K. (2006) Structures of the high-valent metal-ion haem-oxygen intermediates in peroxidases, oxygenases and catalases J. Inorg. Biochem. 100, 460-476
    • (2006) J. Inorg. Biochem. , vol.100 , pp. 460-476
    • Hersleth, H.-P.1    Ryde, U.2    Rydberg, P.3    Görbitz, C.H.4    Andersson, K.K.5
  • 78
    • 0016904218 scopus 로고
    • Superoxide dismutases: Studies of structure and mechanism
    • Fridovich, I. (1976) Superoxide dismutases: studies of structure and mechanism Adv. Exp. Med. Biol. 74, 530-539
    • (1976) Adv. Exp. Med. Biol. , vol.74 , pp. 530-539
    • Fridovich, I.1
  • 80
    • 77956257884 scopus 로고    scopus 로고
    • Francisella tularensis antioxidants harness reactive oxygen species to restrict macrophage signaling and cytokine production
    • Melillo, A. A., Bakshi, C. S., and Meléndez, J. A. (2010) Francisella tularensis antioxidants harness reactive oxygen species to restrict macrophage signaling and cytokine production J. Biol. Chem. 285, 27553-27560
    • (2010) J. Biol. Chem. , vol.285 , pp. 27553-27560
    • Melillo, A.A.1    Bakshi, C.S.2    Meléndez, J.A.3
  • 82
    • 58449102794 scopus 로고    scopus 로고
    • SodA is essential for virulence of Borrelia burgdorferi in the murine model of Lyme disease
    • Esteve-Gassent, M. D., Elliott, N. L., and Seshu, J. (2009) SodA is essential for virulence of Borrelia burgdorferi in the murine model of Lyme disease Mol. Microbiol. 71, 594-612
    • (2009) Mol. Microbiol. , vol.71 , pp. 594-612
    • Esteve-Gassent, M.D.1    Elliott, N.L.2    Seshu, J.3
  • 83
    • 10044255385 scopus 로고    scopus 로고
    • Involvement of SirABC in iron-siderophore import in Staphylococcus aureus
    • DOI 10.1128/JB.186.24.8356-8362.2004
    • Dale, S. E., Sebulsky, M. T., and Heinrichs, D. E. (2004) Involvement of SirABC in iron-siderophore import in Staphylococcus aureus J. Bacteriol. 186, 8356-8362 (Pubitemid 39603226)
    • (2004) Journal of Bacteriology , vol.186 , Issue.24 , pp. 8356-8362
    • Dale, S.E.1    Sebulsky, M.T.2    Heinrichs, D.E.3
  • 84
    • 0032743775 scopus 로고    scopus 로고
    • Withholding and exchanging iron: Interactions between Erwinia spp. and their plant hosts
    • DOI 10.1146/annurev.phyto.37.1.307
    • Expert, D. (1999) Withholding and exchanging iron: Interactions between Erwinia spp. and their plant hosts Annu. Rev. Phytopathol. 37, 307-334 (Pubitemid 29523938)
    • (1999) Annual Review of Phytopathology , vol.37 , pp. 307-334
    • Expert, D.1
  • 85
    • 62449171768 scopus 로고    scopus 로고
    • Roles of the extraintestinal pathogenic Escherichia coli ZnuACB and ZupT zinc transporters during urinary tract infection
    • Sabri, M., Houle, S., and Dozois, C. M. (2009) Roles of the extraintestinal pathogenic Escherichia coli ZnuACB and ZupT zinc transporters during urinary tract infection Infect. Immun. 77, 1155-1164
    • (2009) Infect. Immun. , vol.77 , pp. 1155-1164
    • Sabri, M.1    Houle, S.2    Dozois, C.M.3
  • 86
    • 79961103204 scopus 로고    scopus 로고
    • A novel Zinc binding system, ZevAB, is critical for survival of nontypeable Haemophilus influenzae in a murine lung infection model
    • Rosadini, C. V., Gawronski, J. D., Raimunda, D., Argüello, J. M., and Akerley, B. J. (2011) A novel Zinc binding system, ZevAB, is critical for survival of nontypeable Haemophilus influenzae in a murine lung infection model Infect. Immun. 79, 3366-3376
    • (2011) Infect. Immun. , vol.79 , pp. 3366-3376
    • Rosadini, C.V.1    Gawronski, J.D.2    Raimunda, D.3    Argüello, J.M.4    Akerley, B.J.5
  • 87
    • 0027262167 scopus 로고
    • Natural resistance to infection with intracellular parasites: Isolation of a candidate for Bcg
    • DOI 10.1016/0092-8674(93)90135-D
    • Vidal, S. M., Malo, D., Vogan, K., Skamene, E., and Gros, P. (1993) Natural resistance to infection with intracellular parasites: Isolation of a candidate for Bcg Cell 73, 469-485 (Pubitemid 23143347)
    • (1993) Cell , vol.73 , Issue.3 , pp. 469-485
    • Vidal, S.M.1    Malo, D.2    Vogan, K.3    Skamene, E.4    Gros, P.5
  • 88
    • 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
  • 89
    • 77958516886 scopus 로고    scopus 로고
    • The phage shock protein PspA facilitates divalent metal transport and is required for virulence of Salmonella enterica sv. Typhimurium
    • Karlinsey, J. E., Maguire, M. E., Becker, L. A., Crouch, M.-L. V., and Fang, F. C. (2010) The phage shock protein PspA facilitates divalent metal transport and is required for virulence of Salmonella enterica sv. Typhimurium Mol. Microbiol. 78, 669-685
    • (2010) Mol. Microbiol. , vol.78 , pp. 669-685
    • Karlinsey, J.E.1    Maguire, M.E.2    Becker, L.A.3    Crouch, M.-L.V.4    Fang, F.C.5
  • 90
    • 12444344631 scopus 로고    scopus 로고
    • Elemental analysis of Mycobacterium avium-, Mycobacterium tuberculosis-, and Mycobacterium smegmatis -containing phagosomes indicates pathogen-induced microenvironments within the host cell endosomal system
    • Wagner, D., Maser, J., Lai, B., Cai, Z., Barry, C. E., Höner Zu Bentrup, K., Russell, D. G., and Bermudez, L. E. (2005) Elemental analysis of Mycobacterium avium-, Mycobacterium tuberculosis-, and Mycobacterium smegmatis -containing phagosomes indicates pathogen-induced microenvironments within the host cell endosomal system J. Immunol. 174, 1491-1500
    • (2005) J. Immunol. , vol.174 , pp. 1491-1500
    • Wagner, D.1    Maser, J.2    Lai, B.3    Cai, Z.4    Barry, C.E.5    Höner Zu Bentrup, K.6    Russell, D.G.7    Bermudez, L.E.8
  • 91
    • 71749115454 scopus 로고    scopus 로고
    • A role for the ATP7A copper-transporting ATPase in macrophage bactericidal activity
    • White, C., Lee, J., Kambe, T., Fritsche, K., and Petris, M. J. (2009) A role for the ATP7A copper-transporting ATPase in macrophage bactericidal activity J. Biol. Chem. 284, 33949-33956
    • (2009) J. Biol. Chem. , vol.284 , pp. 33949-33956
    • White, C.1    Lee, J.2    Kambe, T.3    Fritsche, K.4    Petris, M.J.5
  • 92
    • 78049471498 scopus 로고    scopus 로고
    • The bacterial pathogen Xanthomonas oryzae overcomes rice defenses by regulating host copper redistribution
    • Yuan, M., Chu, Z., Li, X., Xu, C., and Wang, S. (2010) The bacterial pathogen Xanthomonas oryzae overcomes rice defenses by regulating host copper redistribution Plant Cell 22, 3164-3176
    • (2010) Plant Cell , vol.22 , pp. 3164-3176
    • Yuan, M.1    Chu, Z.2    Li, X.3    Xu, C.4    Wang, S.5
  • 93
    • 7744237723 scopus 로고    scopus 로고
    • Cuprous oxidase activity of CueO from Escherichia coli
    • DOI 10.1128/JB.186.22.7815-7817.2004
    • Singh, S. K., Grass, G., Rensing, C., and Montfort, W. R. (2004) Cuprous oxidase activity of CueO from Escherichia coli J. Bacteriol. 186, 7815-7817 (Pubitemid 39463750)
    • (2004) Journal of Bacteriology , vol.186 , Issue.22 , pp. 7815-7817
    • Singh, S.K.1    Grass, G.2    Rensing, C.3    Montfort, W.R.4
  • 97
    • 0030663234 scopus 로고    scopus 로고
    • Respiratory protection of nitrogenase activity in Azotobacter vinelandii - Roles of the terminal oxidases
    • DOI 10.1023/A:1027336712748
    • Poole, R. K. and Hill, S. (1997) Respiratory protection of nitrogenase activity in Azotobacter vinelandii-roles of the terminal oxidases Biosci. Rep. 17, 303-317 (Pubitemid 27466754)
    • (1997) Bioscience Reports , vol.17 , Issue.3 , pp. 303-317
    • Poole, R.K.1    Hill, S.2
  • 100
    • 0012368447 scopus 로고
    • The role of copper in citriculture
    • Alva, A. K. and Graham, J. H. (1991) The role of copper in citriculture Adv. Agron. 1, 145-170
    • (1991) Adv. Agron. , vol.1 , pp. 145-170
    • Alva, A.K.1    Graham, J.H.2
  • 102
  • 103
    • 33745444060 scopus 로고    scopus 로고
    • FixJ: A major regulator of the oxygen limitation response and late symbiotic functions of Sinorhizobium meliloti
    • DOI 10.1128/JB.00251-06
    • Bobik, C., Meilhoc, E., and Batut, J. (2006) FixJ: a major regulator of the oxygen limitation response and late symbiotic functions of Sinorhizobium meliloti J. Bacteriol. 188, 4890-4902 (Pubitemid 43956087)
    • (2006) Journal of Bacteriology , vol.188 , Issue.13 , pp. 4890-4902
    • Bobik, C.1    Meilhoc, E.2    Batut, J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.