메뉴 건너뛰기




Volumn 47, Issue 12, 2014, Pages 3605-3613

Copper transport and trafficking at the host-bacterial pathogen interface

Author keywords

[No Author keywords available]

Indexed keywords

COPPER;

EID: 84918555449     PISSN: 00014842     EISSN: 15204898     Source Type: Journal    
DOI: 10.1021/ar500300n     Document Type: Article
Times cited : (99)

References (64)
  • 1
    • 84892841021 scopus 로고    scopus 로고
    • Recent developments in copper and zinc homeostasis in bacterial pathogens
    • Braymer, J. J.; Giedroc, D. P. Recent developments in copper and zinc homeostasis in bacterial pathogens. Curr. Opin. Chem. Biol. 2014, 19, 59-66.
    • (2014) Curr. Opin. Chem. Biol. , vol.19 , pp. 59-66
    • Braymer, J.J.1    Giedroc, D.P.2
  • 3
  • 4
    • 84255178757 scopus 로고    scopus 로고
    • Coordination chemistry of copper proteins: How nature handles a toxic cargo for essential function
    • Rubino, J. T.; Franz, K. J. Coordination chemistry of copper proteins: How nature handles a toxic cargo for essential function. J. Inorg. Biochem. 2012, 107, 129-143.
    • (2012) J. Inorg. Biochem. , vol.107 , pp. 129-143
    • Rubino, J.T.1    Franz, K.J.2
  • 5
    • 33947364844 scopus 로고    scopus 로고
    • Intracellular copper does not catalyze the formation of oxidative DNA damage in Escherichia coli
    • Macomber, L.; Rensing, C.; Imlay, J. A. Intracellular copper does not catalyze the formation of oxidative DNA damage in Escherichia coli. J. Bacteriol. 2007, 189, 1616-1626.
    • (2007) J. Bacteriol. , vol.189 , pp. 1616-1626
    • Macomber, L.1    Rensing, C.2    Imlay, J.A.3
  • 6
    • 66249112833 scopus 로고    scopus 로고
    • The iron-sulfur clusters of dehydratases are primary intracellular targets of copper toxicity
    • Macomber, L.; Imlay, J. A. The iron-sulfur clusters of dehydratases are primary intracellular targets of copper toxicity. Proc. Natl. Acad. Sci. U. S. A. 2009, 106, 8344-8349.
    • (2009) Proc. Natl. Acad. Sci. U. S. A. , vol.106 , pp. 8344-8349
    • Macomber, L.1    Imlay, J.A.2
  • 7
    • 77952056332 scopus 로고    scopus 로고
    • Copper stress affects iron homeostasis by destabilizing iron-sulfur cluster formation in Bacillus subtilis
    • Chillappagari, S.; Seubert, A.; Trip, H.; Kuipers, O. P.; Marahiel, M. A.; Miethke, M. Copper stress affects iron homeostasis by destabilizing iron-sulfur cluster formation in Bacillus subtilis. J. Bacteriol. 2010, 192, 2512-2524.
    • (2010) J. Bacteriol. , vol.192 , pp. 2512-2524
    • Chillappagari, S.1    Seubert, A.2    Trip, H.3    Kuipers, O.P.4    Marahiel, M.A.5    Miethke, M.6
  • 8
    • 84876199009 scopus 로고    scopus 로고
    • Coproporphyrin III excretion identifies the anaerobic coproporphyrinogen III oxidase HemN as a copper target in the Cu(+)-ATPase mutant copA(-) of Rubrivivax gelatinosus
    • Azzouzi, A.; Steunou, A. S.; Durand, A.; Khalfaoui-Hassani, B.; Bourbon, M. L.; Astier, C.; Bollivar, D. W.; Ouchane, S. Coproporphyrin III excretion identifies the anaerobic coproporphyrinogen III oxidase HemN as a copper target in the Cu(+)-ATPase mutant copA(-) of Rubrivivax gelatinosus. Mol. Microbiol. 2013, 88, 339-351.
    • (2013) Mol. Microbiol. , vol.88 , pp. 339-351
    • Azzouzi, A.1    Steunou, A.S.2    Durand, A.3    Khalfaoui-Hassani, B.4    Bourbon, M.L.5    Astier, C.6    Bollivar, D.W.7    Ouchane, S.8
  • 9
    • 84886505032 scopus 로고    scopus 로고
    • Antimicrobial action of copper is amplified via inhibition of heme biosynthesis
    • Djoko, K. Y.; McEwan, A. G. Antimicrobial action of copper is amplified via inhibition of heme biosynthesis. ACS Chem. Biol. 2013, 8, 2217-2223.
    • (2013) ACS Chem. Biol. , vol.8 , pp. 2217-2223
    • Djoko, K.Y.1    McEwan, A.G.2
  • 10
    • 78649642416 scopus 로고    scopus 로고
    • Instability of ackA (acetate kinase) mutations and their effects on acetyl phosphate and ATP amounts in Streptococcus pneumoniae D39
    • Ramos-Montanez, S.; Kazmierczak, K. M.; Hentchel, K. L.; Winkler, M. E. Instability of ackA (acetate kinase) mutations and their effects on acetyl phosphate and ATP amounts in Streptococcus pneumoniae D39. J. Bacteriol. 2010, 192, 6390-6400.
    • (2010) J. Bacteriol. , vol.192 , pp. 6390-6400
    • Ramos-Montanez, S.1    Kazmierczak, K.M.2    Hentchel, K.L.3    Winkler, M.E.4
  • 11
    • 77949917893 scopus 로고    scopus 로고
    • Human copper homeostasis: A network of interconnected pathways
    • Lutsenko, S. Human copper homeostasis: A network of interconnected pathways. Curr..Opin. Chem. Biol. 2010, 14, 211-217.
    • (2010) Curr..Opin. Chem. Biol. , vol.14 , pp. 211-217
    • Lutsenko, S.1
  • 12
    • 0033617578 scopus 로고    scopus 로고
    • Undetectable intracellular free copper: The Requirement of a copper chaperone for superoxide dismutase
    • Rae, T. D.; Schmidt, P. J.; Pufahl, R. A.; Culotta, V. C.; V. O'Halloran, T. Undetectable intracellular free copper: The Requirement of a copper chaperone for superoxide dismutase. Science 1999, 284, 805-808.
    • (1999) Science , vol.284 , pp. 805-808
    • Rae, T.D.1    Schmidt, P.J.2    Pufahl, R.A.3    Culotta, V.C.4    O'Halloran, T.V.5
  • 13
    • 70350627430 scopus 로고    scopus 로고
    • Structural biology of copper trafficking
    • Boal, A. K.; Rosenzweig, A. C. Structural biology of copper trafficking. Chem. Rev. 2009, 109, 4760-4779.
    • (2009) Chem. Rev. , vol.109 , pp. 4760-4779
    • Boal, A.K.1    Rosenzweig, A.C.2
  • 14
    • 1642404510 scopus 로고    scopus 로고
    • C-terminal domain of the membrane copper transporter Ctr1 from Saccharomyces cerevisiae binds four Cu(I) ions as a cuprous-thiolate polynuclear cluster: Sub-femtomolar Cu(I) affinity of three proteins involved in copper trafficking
    • Xiao, Z.; Loughlin, F.; George, G. N.; Howlett, G. J.; Wedd, A. G. C-terminal domain of the membrane copper transporter Ctr1 from Saccharomyces cerevisiae binds four Cu(I) ions as a cuprous-thiolate polynuclear cluster: Sub-femtomolar Cu(I) affinity of three proteins involved in copper trafficking. J. Am. Chem. Soc. 2004, 126, 3081-3090.
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 3081-3090
    • Xiao, Z.1    Loughlin, F.2    George, G.N.3    Howlett, G.J.4    Wedd, A.G.5
  • 15
    • 84878653071 scopus 로고    scopus 로고
    • Cellular glutathione plays a key role in copper uptake mediated by human copper transporter 1
    • Maryon, E. B.; Malloy, S. A.; Kaplan, J. H. Cellular glutathione plays a key role in copper uptake mediated by human copper transporter 1. Am. J. Physiol.: Cell Physiol. 2013, 304, C768-C779.
    • (2013) Am. J. Physiol.: Cell Physiol. , vol.304 , pp. C768-C779
    • Maryon, E.B.1    Malloy, S.A.2    Kaplan, J.H.3
  • 16
    • 84888301851 scopus 로고    scopus 로고
    • Atox1 contains positive residues that mediate membrane association and aid subsequent copper loading
    • Flores, A.; Unger, V. Atox1 contains positive residues that mediate membrane association and aid subsequent copper loading. J. Membr. Biol. 2013, 246, 903-913.
    • (2013) J. Membr. Biol. , vol.246 , pp. 903-913
    • Flores, A.1    Unger, V.2
  • 18
    • 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.; Petris, M. J. A role for the ATP7A copper-transporting ATPase in macrophage bactericidal activity. J. Biol. Chem. 2009, 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
  • 21
    • 50549086197 scopus 로고    scopus 로고
    • Interferon-gamma limits the availability of iron for intramacrophage Salmonellta typhimurium
    • Nairz, M.; Fritsche, G.; Brunner, P.; Talasz, H.; Hantke, K.; Weiss, G. Interferon-gamma limits the availability of iron for intramacrophage Salmonellta typhimurium. Eur. J. Immunol. 2008, 38, 1923-1936.
    • (2008) Eur. J. Immunol. , vol.38 , pp. 1923-1936
    • Nairz, M.1    Fritsche, G.2    Brunner, P.3    Talasz, H.4    Hantke, K.5    Weiss, G.6
  • 25
    • 4043057281 scopus 로고    scopus 로고
    • Unique features of the sodC-encoded superoxide dismutase from Mycobacterium tuberculosis, a fully functional copper-containing enzyme lacking zinc in the active site
    • Spagnolo, L.; Toro, I.; D'Orazio, M.; O 'Neill, P.; Pedersen, J. Z.; Carugo, O.; Rotilio, G.; Battistoni, A.; Djinovic-Carugo, K. Unique features of the sodC-encoded superoxide dismutase from Mycobacterium tuberculosis, a fully functional copper-containing enzyme lacking zinc in the active site. J. Biol. Chem. 2004, 279, 33447-33455.
    • (2004) J. Biol. Chem. , vol.279 , pp. 33447-33455
    • Spagnolo, L.1    Toro, I.2    D'Orazio, M.3    'Neill P, O.4    Pedersen, J.Z.5    Carugo, O.6    Rotilio, G.7    Battistoni, A.8    Djinovic-Carugo, K.9
  • 26
    • 57649185429 scopus 로고    scopus 로고
    • N-Terminal clustering of the Oglycosylation sites in the Mycobacterium tuberculosis lipoprotein SodC
    • Sartain, M. J.; Belisle, J. T. N-Terminal clustering of the Oglycosylation sites in the Mycobacterium tuberculosis lipoprotein SodC. Glycobiology 2009, 19, 38-51.
    • (2009) Glycobiology , vol.19 , pp. 38-51
    • Sartain, M.J.1    Belisle, J.T.2
  • 28
    • 64049083159 scopus 로고    scopus 로고
    • Copper acquisition is mediated by YcnJ and regulated by YcnK and CsoR in Bacillus subtilis
    • Chillappagari, S.; Miethke, M.; Trip, H.; Kuipers, O. P.; Marahiel, M. A. Copper acquisition is mediated by YcnJ and regulated by YcnK and CsoR in Bacillus subtilis. J. Bacteriol. 2009, 191, 2362-2370.
    • (2009) J. Bacteriol. , vol.191 , pp. 2362-2370
    • Chillappagari, S.1    Miethke, M.2    Trip, H.3    Kuipers, O.P.4    Marahiel, M.A.5
  • 29
    • 80455176470 scopus 로고    scopus 로고
    • Copper toxicity and the origin of bacterial resistance-new insights and applications
    • Dupont, C. L.; Grass, G.; Rensing, C. Copper toxicity and the origin of bacterial resistance-new insights and applications. Metallomics 2011, 3, 1109-1118.
    • (2011) Metallomics , vol.3 , pp. 1109-1118
    • Dupont, C.L.1    Grass, G.2    Rensing, C.3
  • 30
    • 70350637580 scopus 로고    scopus 로고
    • Coordination chemistry of bacterial metal transport and sensing
    • Ma, Z.; Jacobsen, F. E.; Giedroc, D. P. Coordination chemistry of bacterial metal transport and sensing. Chem. Rev. 2009, 109, 4644-4681.
    • (2009) Chem. Rev. , vol.109 , pp. 4644-4681
    • Ma, Z.1    Jacobsen, F.E.2    Giedroc, D.P.3
  • 32
    • 84867158886 scopus 로고    scopus 로고
    • Metal export by CusCFBA, the periplasmic Cu(I)/Ag(I) transport system of Escherichia coli
    • Mealman, T. D.; Blackburn, N. J.; McEvoy, M. M. Metal export by CusCFBA, the periplasmic Cu(I)/Ag(I) transport system of Escherichia coli. Curr. Top. Membr. 2012, 69, 163-196.
    • (2012) Curr. Top. Membr. , vol.69 , pp. 163-196
    • Mealman, T.D.1    Blackburn, N.J.2    McEvoy, M.M.3
  • 33
    • 0037701544 scopus 로고    scopus 로고
    • Molecular analysis of the copper-transporting efflux system CusCFBA of Escherichia coli
    • Franke, S.; Grass, G.; Rensing, C.; Nies, D. H. Molecular analysis of the copper-transporting efflux system CusCFBA of Escherichia coli. J. Bacteriol. 2003, 185, 3804-3812.
    • (2003) J. Bacteriol. , vol.185 , pp. 3804-3812
    • Franke, S.1    Grass, G.2    Rensing, C.3    Nies, D.H.4
  • 35
    • 55249109759 scopus 로고    scopus 로고
    • Direct metal transfer between periplasmic proteins identifies a bacterial copper chaperone
    • Bagai, I.; Rensing, C.; Blackburn, N. J.; McEvoy, M. M. Direct metal transfer between periplasmic proteins identifies a bacterial copper chaperone. Biochemistry 2008, 47, 11408-11414.
    • (2008) Biochemistry , vol.47 , pp. 11408-11414
    • Bagai, I.1    Rensing, C.2    Blackburn, N.J.3    McEvoy, M.M.4
  • 36
    • 79953171122 scopus 로고    scopus 로고
    • Interactions between CusF and CusB identified by NMR spectroscopy and chemical crosslinking coupled to mass spectrometry
    • Mealman, T. D.; Bagai, I.; Singh, P.; Goodlett, D. R.; Rensing, C.; Zhou, H.; Wysocki, V. H.; McEvoy, M. M. Interactions between CusF and CusB identified by NMR spectroscopy and chemical crosslinking coupled to mass spectrometry. Biochemistry 2011, 50, 2559-2566.
    • (2011) Biochemistry , vol.50 , pp. 2559-2566
    • Mealman, T.D.1    Bagai, I.2    Singh, P.3    Goodlett, D.R.4    Rensing, C.5    Zhou, H.6    Wysocki, V.H.7    McEvoy, M.M.8
  • 37
    • 84908425792 scopus 로고    scopus 로고
    • Tracking metal ions through a Cu/Ag efflux pump assigns the functional roles of the periplasmic proteins
    • in press
    • Chacon, K. N.; Mealman, T. D.; McEvoy, M. M.; Blackburn, N. J. Tracking metal ions through a Cu/Ag efflux pump assigns the functional roles of the periplasmic proteins. Proc. Natl. Acad. Sci. U. S. A. 2014, in press.
    • (2014) Proc. Natl. Acad. Sci. U. S. A.
    • Chacon, K.N.1    Mealman, T.D.2    McEvoy, M.M.3    Blackburn, N.J.4
  • 38
    • 39449113042 scopus 로고    scopus 로고
    • A place for thioether chemistry in cellular copper ion recognition and trafficking
    • Davis, A. V.; O 'Halloran, T. V. A place for thioether chemistry in cellular copper ion recognition and trafficking. Nat. Chem. Biol. 2008, 4, 148-151.
    • (2008) Nat. Chem. Biol. , vol.4 , pp. 148-151
    • Davis, A.V.1    O'Halloran, T.V.2
  • 39
    • 84905402461 scopus 로고    scopus 로고
    • Mechanism of ATPase-mediated Cu+ export and delivery to periplasmic chaperones: The interaction of Escherichia coli CopA and CusF
    • Padilla-Benavides, T.; George Thompson, A. M.; McEvoy, M. M.; Arguello, J. M. Mechanism of ATPase-mediated Cu+ export and delivery to periplasmic chaperones: The interaction of Escherichia coli CopA and CusF. J. Biol. Chem. 2014, 289, 20492-20501.
    • (2014) J. Biol. Chem. , vol.289 , pp. 20492-20501
    • Padilla-Benavides, T.1    George Thompson, A.M.2    McEvoy, M.M.3    Arguello, J.M.4
  • 40
    • 84859425452 scopus 로고    scopus 로고
    • Regulation of Cu(I)/Ag(I) efflux genes in Escherichia coli by the sensor kinase CusS
    • Gudipaty, S. A.; Larsen, A. S.; Rensing, C.; McEvoy, M. M. Regulation of Cu(I)/Ag(I) efflux genes in Escherichia coli by the sensor kinase CusS. FEMS Microbiol. Lett. 2012, 330, 30-37.
    • (2012) FEMS Microbiol. Lett. , vol.330 , pp. 30-37
    • Gudipaty, S.A.1    Larsen, A.S.2    Rensing, C.3    McEvoy, M.M.4
  • 41
    • 67650436140 scopus 로고    scopus 로고
    • Alternative periplasmic copperresistance mechanisms in Gram negative bacteria
    • Pontel, L. B.; Soncini, F. C. Alternative periplasmic copperresistance mechanisms in Gram negative bacteria. Mol. Microbiol. 2009, 73, 212-225.
    • (2009) Mol. Microbiol. , vol.73 , pp. 212-225
    • Pontel, L.B.1    Soncini, F.C.2
  • 43
    • 84873060682 scopus 로고    scopus 로고
    • The copper supply pathway to a Salmonella Cu,Zn-superoxide dismutase (SodCII) involves P1B-type ATPase copper efflux and periplasmic CueP
    • Osman, D.; Patterson, C. J.; Bailey, K.; Fisher, K.; Robinson, N. J.; Rigby, S. E. J.; Cavet, J. S. The copper supply pathway to a Salmonella Cu,Zn-superoxide dismutase (SodCII) involves P1B-type ATPase copper efflux and periplasmic CueP. Mol. Microbiol. 2013, 87, 466-477.
    • (2013) Mol. Microbiol. , vol.87 , pp. 466-477
    • Osman, D.1    Patterson, C.J.2    Bailey, K.3    Fisher, K.4    Robinson, N.J.5    Rigby, S.E.J.6    Cavet, J.S.7
  • 44
    • 43149096496 scopus 로고    scopus 로고
    • Mechanism of Cu +-transporting ATPases: Soluble Cu+ chaperones directly transfer Cu+ to transmembrane transport sites
    • Gonzalez-Guerrero, M.; Arguello, J. M. Mechanism of Cu +-transporting ATPases: soluble Cu+ chaperones directly transfer Cu+ to transmembrane transport sites. Proc. Natl. Acad. Sci. U. S. A. 2008, 105, 5992-5997.
    • (2008) Proc. Natl. Acad. Sci. U. S. A. , vol.105 , pp. 5992-5997
    • Gonzalez-Guerrero, M.1    Arguello, J.M.2
  • 47
    • 79960177773 scopus 로고    scopus 로고
    • The combined actions of the copper-responsive repressor CsoR and copper-metallochaperone CopZ modulate CopA-mediated copper efflux in the intracellular pathogen Listeria monocytogenes
    • Corbett, D.; Schuler, S.; Glenn, S.; Andrew, P. W.; Cavet, J. S.; Roberts, I. S. The combined actions of the copper-responsive repressor CsoR and copper-metallochaperone CopZ modulate CopA-mediated copper efflux in the intracellular pathogen Listeria monocytogenes. Mol. Microbiol. 2011, 81, 457-472.
    • (2011) Mol. Microbiol. , vol.81 , pp. 457-472
    • Corbett, D.1    Schuler, S.2    Glenn, S.3    Andrew, P.W.4    Cavet, J.S.5    Roberts, I.S.6
  • 52
    • 84872072402 scopus 로고    scopus 로고
    • The mechanism of Cu+ transport ATPases: Interaction with Cu+ chaperones and the role of transient metal-binding sites
    • Padilla-Benavides, T.; McCann, C. J.; Argüello, J. M. The mechanism of Cu+ transport ATPases: Interaction with Cu+ chaperones and the role of transient metal-binding sites. J. Biol. Chem. 2013, 288, 69-78.
    • (2013) J. Biol. Chem. , vol.288 , pp. 69-78
    • Padilla-Benavides, T.1    McCann, C.J.2    Argüello, J.M.3
  • 54
    • 84863899006 scopus 로고    scopus 로고
    • Nutritional immunity: Transition metals at the pathogen-host interface
    • Hood, M. I.; Skaar, E. P. Nutritional immunity: Transition metals at the pathogen-host interface. Nat. Rev. Microbiol. 2012, 10, 525-537.
    • (2012) Nat. Rev. Microbiol. , vol.10 , pp. 525-537
    • Hood, M.I.1    Skaar, E.P.2
  • 55
    • 84864554815 scopus 로고    scopus 로고
    • Functional partnership of the copper export machinery and glutathione balance in human cells
    • Hatori, Y.; Clasen, S.; Hasan, N. M.; Barry, A. N.; Lutsenko, S. Functional partnership of the copper export machinery and glutathione balance in human cells. J. Biol. Chem. 2012, 287, 26678-26687.
    • (2012) J. Biol. Chem. , vol.287 , pp. 26678-26687
    • Hatori, Y.1    Clasen, S.2    Hasan, N.M.3    Barry, A.N.4    Lutsenko, S.5
  • 56
    • 84897381356 scopus 로고    scopus 로고
    • Redox sulfur chemistry of the copper chaperone Atox1 is regulated by the enzyme glutaredoxin 1, the reduction potential of the glutathione couple GSSG/2GSH and the availability of Cu(I)
    • Brose, J.; La Fontaine, S.; Wedd, A. G.; Xiao, Z. Redox sulfur chemistry of the copper chaperone Atox1 is regulated by the enzyme glutaredoxin 1, the reduction potential of the glutathione couple GSSG/2GSH and the availability of Cu(I). Metallomics 2014, 6, 793-808.
    • (2014) Metallomics , vol.6 , pp. 793-808
    • Brose, J.1    La Fontaine, S.2    Wedd, A.G.3    Xiao, Z.4
  • 58
    • 48149108241 scopus 로고    scopus 로고
    • Glutathione and transition-metal homeostasis in Escherichia coli
    • Helbig, K.; Bleuel, C.; Krauss, G. J.; Nies, D. H. Glutathione and transition-metal homeostasis in Escherichia coli. J. Bacteriol. 2008, 190, 5431-5438.
    • (2008) J. Bacteriol. , vol.190 , pp. 5431-5438
    • Helbig, K.1    Bleuel, C.2    Krauss, G.J.3    Nies, D.H.4
  • 59
    • 84869105723 scopus 로고    scopus 로고
    • Streptococcus pneumoniae uses glutathione to defend against oxidative stress and metal ion toxicity
    • Potter, A. J.; Trappetti, C.; Paton, J. C. Streptococcus pneumoniae uses glutathione to defend against oxidative stress and metal ion toxicity. J. Bacteriol. 2012, 194, 6248-6254.
    • (2012) J. Bacteriol. , vol.194 , pp. 6248-6254
    • Potter, A.J.1    Trappetti, C.2    Paton, J.C.3
  • 60
    • 84881013236 scopus 로고    scopus 로고
    • A multicopper oxidase is required for copper resistance in Mycobacterium tuberculosis
    • Rowland, J. L.; Niederweis, M. A multicopper oxidase is required for copper resistance in Mycobacterium tuberculosis. J. Bacteriol. 2013, 195, 3724-3733.
    • (2013) J. Bacteriol. , vol.195 , pp. 3724-3733
    • Rowland, J.L.1    Niederweis, M.2
  • 61
    • 77956150312 scopus 로고    scopus 로고
    • CtpV: A putative copper exporter required for full virulence of Mycobacterium tuberculosis
    • Ward, S. K.; Abomoelak, B.; Hoye, E. A.; Steinberg, H.; Talaat, A. M. CtpV: A putative copper exporter required for full virulence of Mycobacterium tuberculosis. Mol. Microbiol. 2010, 77, 1096-1110.
    • (2010) Mol. Microbiol. , vol.77 , pp. 1096-1110
    • Ward, S.K.1    Abomoelak, B.2    Hoye, E.A.3    Steinberg, H.4    Talaat, A.M.5
  • 64
    • 33646544710 scopus 로고    scopus 로고
    • Intermolecular transfer of copper ions from the CopC protein of Pseudomonas syringae. Crystal structures of fully loaded Cu(I)Cu(II) forms
    • Zhang, L.; Koay, M.; Maher, M. J.; Xiao, Z.; Wedd, A. G. Intermolecular transfer of copper ions from the CopC protein of Pseudomonas syringae. Crystal structures of fully loaded Cu(I)Cu(II) forms. J. Am. Chem. Soc. 2006, 128, 5834-5850.
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 5834-5850
    • Zhang, L.1    Koay, M.2    Maher, M.J.3    Xiao, Z.4    Wedd, A.G.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.