메뉴 건너뛰기




Volumn 53, Issue 4, 2013, Pages 303-317

Microbial siderophores: A mini review

Author keywords

Chelator; Iron; Microbes; Siderophores

Indexed keywords

IRON; SIDEROPHORE;

EID: 84876426944     PISSN: 0233111X     EISSN: 15214028     Source Type: Journal    
DOI: 10.1002/jobm.201100552     Document Type: Article
Times cited : (297)

References (209)
  • 1
    • 0019759560 scopus 로고
    • Iron absorption and transport in microorganisms
    • Neilands, J.B., 1981. Iron absorption and transport in microorganisms. Annu. Rev. Nutr. 1, 27-46.
    • (1981) Annu. Rev. Nutr. , vol.1 , pp. 27-46
    • Neilands, J.B.1
  • 2
    • 0019348762 scopus 로고
    • Microbial iron compounds
    • Neilands, J.B., 1981. Microbial iron compounds. Annu. Rev. Biochem. 50, 715-731.
    • (1981) Annu. Rev. Biochem. , vol.50 , pp. 715-731
    • Neilands, J.B.1
  • 3
    • 0028850367 scopus 로고
    • Siderophores: structure and function of microbial Iron transport compounds
    • Neilands, J.B., 1995. Siderophores: structure and function of microbial Iron transport compounds. J. Biol. Chem. 270, 26723-26726.
    • (1995) J. Biol. Chem. , vol.270 , pp. 26723-26726
    • Neilands, J.B.1
  • 4
    • 0024404842 scopus 로고
    • Genetics and molecular biology of siderophore-mediated iron transport in bacteria
    • Crosa, J.H., 1989. Genetics and molecular biology of siderophore-mediated iron transport in bacteria. Microbiol. Molbiol. Rev. 53, 517-530.
    • (1989) Microbiol. Molbiol. Rev. , vol.53 , pp. 517-530
    • Crosa, J.H.1
  • 5
    • 0037389797 scopus 로고    scopus 로고
    • Enterobactin: an archetype for microbial iron transport
    • Raymond, K.N., Dertz, E.A., Kim, S.S., 2003. Enterobactin: an archetype for microbial iron transport. Proc. Natl. Acad. Sci. 100, 3584-3588.
    • (2003) Proc. Natl. Acad. Sci. , vol.100 , pp. 3584-3588
    • Raymond, K.N.1    Dertz, E.A.2    Kim, S.S.3
  • 6
    • 0021190269 scopus 로고
    • The relationship of plasmid-mediated iron transport and bacterial virulence
    • Crosa, J.H., 1984. The relationship of plasmid-mediated iron transport and bacterial virulence. Annu. Rev. Microbiol. 38, 69-89.
    • (1984) Annu. Rev. Microbiol. , vol.38 , pp. 69-89
    • Crosa, J.H.1
  • 7
    • 31844433824 scopus 로고    scopus 로고
    • Biochemical and physical properties of siderophores
    • Crosa, J.M., Mey, A.M., Pyne, S.M., eds., ASM Press, Washington DC
    • Raymond, K., Dertz, E.M., 2004. Biochemical and physical properties of siderophores. In: Crosa, J.M., Mey, A.M., Pyne, S.M., (eds.), Iron Transport in Bacteria. ASM Press, Washington DC, pp. 1-16.
    • (2004) Iron Transport in Bacteria , pp. 1-16
    • Raymond, K.1    Dertz, E.M.2
  • 8
    • 77958143617 scopus 로고    scopus 로고
    • The battle for iron between bacterial pathogens and their vertebrate hosts
    • Skaar, E.P., 2010. The battle for iron between bacterial pathogens and their vertebrate hosts. PLoS Pathog. 6, e1000949.
    • (2010) PLoS Pathog. , vol.6
    • Skaar, E.P.1
  • 9
    • 0020346483 scopus 로고
    • Microbial envelope proteins related to iron
    • Neilands, J.B., 1982. Microbial envelope proteins related to iron. Annu. Rev. Microbiol. 36, 285-309.
    • (1982) Annu. Rev. Microbiol. , vol.36 , pp. 285-309
    • Neilands, J.B.1
  • 10
    • 34548739613 scopus 로고    scopus 로고
    • Siderophore-based iron acquisition and pathogen control
    • Miethke, M., Marahiel, M.A., 2007. Siderophore-based iron acquisition and pathogen control. Microbiol. Molbiol. Rev. 71, 413-451.
    • (2007) Microbiol. Molbiol. Rev. , vol.71 , pp. 413-451
    • Miethke, M.1    Marahiel, M.A.2
  • 11
    • 67651247598 scopus 로고    scopus 로고
    • Is drug release necessary for antimicrobial activity of siderophore-drug conjugates? Syntheses and biological studies of the naturally occurring salmycin "Trojan Horse" antibiotics and synthetic desferridanoxamine-antibiotic conjugates
    • Wencewicz, T., Möllmann, U., Long, T., Miller, M., 2009. Is drug release necessary for antimicrobial activity of siderophore-drug conjugates? Syntheses and biological studies of the naturally occurring salmycin "Trojan Horse" antibiotics and synthetic desferridanoxamine-antibiotic conjugates. BioMetals 22, 633-648.
    • (2009) BioMetals , vol.22 , pp. 633-648
    • Wencewicz, T.1    Möllmann, U.2    Long, T.3    Miller, M.4
  • 12
    • 0018189964 scopus 로고
    • The fluorescent pigment of Pseudomonas fluorescens: biosynthesis, purification and physicochemical properties
    • Meyer, J.M., Abdallah, M.A., 1978. The fluorescent pigment of Pseudomonas fluorescens: biosynthesis, purification and physicochemical properties. J. Gen. Microbiol. 107, 319-328.
    • (1978) J. Gen. Microbiol. , vol.107 , pp. 319-328
    • Meyer, J.M.1    Abdallah, M.A.2
  • 13
    • 0021923023 scopus 로고
    • Siderophore activity of pyoverdine for Pseudomonas aeruginosa
    • Cox, C.D., Adams, P., 1985. Siderophore activity of pyoverdine for Pseudomonas aeruginosa. Infect. Immun. 48, 130.
    • (1985) Infect. Immun. , vol.48 , pp. 130
    • Cox, C.D.1    Adams, P.2
  • 14
    • 0346636767 scopus 로고    scopus 로고
    • Iron acquisition and its control in Pseudomonas aeruginosa: many roads lead to Rome
    • Poole, K., Mckay, G.A., 2003. Iron acquisition and its control in Pseudomonas aeruginosa: many roads lead to Rome. Front. Biosci. 8, 661-686.
    • (2003) Front. Biosci. , vol.8 , pp. 661-686
    • Poole, K.1    Mckay, G.A.2
  • 15
    • 76849108830 scopus 로고    scopus 로고
    • Role of PvdQ in Pseudomonas aeruginosa virulence under iron-limiting conditions
    • Jimenez, P.N., Koch, G., Papaioannou, E., Wahjudi, M. et al., 2010. Role of PvdQ in Pseudomonas aeruginosa virulence under iron-limiting conditions. Microbiology 156, 49-59.
    • (2010) Microbiology , vol.156 , pp. 49-59
    • Jimenez, P.N.1    Koch, G.2    Papaioannou, E.3    Wahjudi, M.4
  • 16
    • 0019588236 scopus 로고
    • Pyochelin: novel structure of an iron-chelating growth promoter for Pseudomonas aeruginosa
    • Cox, C.D., Rinehart, K.L., Moore, M.L., Cook, J.C., 1981. Pyochelin: novel structure of an iron-chelating growth promoter for Pseudomonas aeruginosa. Proc. Natl. Acad. Sci. 78, 4256.
    • (1981) Proc. Natl. Acad. Sci. , vol.78 , pp. 4256
    • Cox, C.D.1    Rinehart, K.L.2    Moore, M.L.3    Cook, J.C.4
  • 17
    • 24644432870 scopus 로고    scopus 로고
    • Crystal structure at high resolution of ferric-pyochelin and its membrane receptor FptA from Pseudomonas aeruginosa
    • Cobessi, D., Celia, H., Pattus, F., 2005. Crystal structure at high resolution of ferric-pyochelin and its membrane receptor FptA from Pseudomonas aeruginosa. J. Mol. Biol. 352, 893-904.
    • (2005) J. Mol. Biol. , vol.352 , pp. 893-904
    • Cobessi, D.1    Celia, H.2    Pattus, F.3
  • 18
    • 66149125265 scopus 로고    scopus 로고
    • The Pseudomonas aeruginosa pyochelin-iron uptake pathway and its metal specificity
    • Braud, A., Hannauer, M., Mislin, G.L.A., Schalk, I.J., 2009. The Pseudomonas aeruginosa pyochelin-iron uptake pathway and its metal specificity. J. Bacteriol. 191, 3517-3525.
    • (2009) J. Bacteriol. , vol.191 , pp. 3517-3525
    • Braud, A.1    Hannauer, M.2    Mislin, G.L.A.3    Schalk, I.J.4
  • 19
    • 0031794801 scopus 로고    scopus 로고
    • Siderotyping of fluorescent pseudomonads:characterization of pyoverdines of Pseudornonas fluorescens and Pseudornonas putida strains from Antarctica
    • Meyer, J-M., Stintzi, A., Coulanges, V., Shivaji, S. et al., 1998. Siderotyping of fluorescent pseudomonads:characterization of pyoverdines of Pseudornonas fluorescens and Pseudornonas putida strains from Antarctica. Microbiology 144, 3119-3126.
    • (1998) Microbiology , vol.144 , pp. 3119-3126
    • Meyer, J.-M.1    Stintzi, A.2    Coulanges, V.3    Shivaji, S.4
  • 20
    • 0036268797 scopus 로고    scopus 로고
    • Siderophore typing, a powerful tool for the identification of fluorescent and nonfluorescent Pseudomonads
    • Meyer, J-M., Geoffroy, V.A., Baida, N., Gardan, L. et al., 2002. Siderophore typing, a powerful tool for the identification of fluorescent and nonfluorescent Pseudomonads. Appl. Environ. Microbiol. 68, 2745-2753.
    • (2002) Appl. Environ. Microbiol. , vol.68 , pp. 2745-2753
    • Meyer, J.-M.1    Geoffroy, V.A.2    Baida, N.3    Gardan, L.4
  • 21
    • 33845951124 scopus 로고    scopus 로고
    • Pyoverdine siderophores: from biogenesis to biosignificance
    • Visca, P., Imperi, F., Lamont, I.L., 2007. Pyoverdine siderophores: from biogenesis to biosignificance. Trends Microbiol. 15, 22-30.
    • (2007) Trends Microbiol. , vol.15 , pp. 22-30
    • Visca, P.1    Imperi, F.2    Lamont, I.L.3
  • 22
    • 0028999977 scopus 로고
    • Iron acquisition by Mycobacterium tuberculosis: isolation and characterization of a family of iron-binding exochelins
    • Gobin, J., Moore, C.H., Reeve, J., Wong, D.K. et al., 1995. Iron acquisition by Mycobacterium tuberculosis: isolation and characterization of a family of iron-binding exochelins. Proc. Natl. Acad. Sci. 92, 5189.
    • (1995) Proc. Natl. Acad. Sci. , vol.92 , pp. 5189
    • Gobin, J.1    Moore, C.H.2    Reeve, J.3    Wong, D.K.4
  • 23
    • 79953175298 scopus 로고    scopus 로고
    • Discovery and characterization of a unique mycobacterial heme acquisition system
    • doi: 10.1073/pnas.1009516108
    • Tullius, M.V., Harmston, C.A., Owens, C.P., Chim, N. et al., 2011. Discovery and characterization of a unique mycobacterial heme acquisition system. Proc. Natl. Acad. Sci. doi: 10.1073/pnas.1009516108
    • (2011) Proc. Natl. Acad. Sci.
    • Tullius, M.V.1    Harmston, C.A.2    Owens, C.P.3    Chim, N.4
  • 24
    • 0002002869 scopus 로고
    • Hydroxamates and polycarboxylates as iron transport agents (siderophores) in fungi
    • Winkelmann, G., Winge, D.R., eds., Marcel Dekker, Inc., New York
    • van der Helm, D., Winkelmann, G., 1994. Hydroxamates and polycarboxylates as iron transport agents (siderophores) in fungi. In: Winkelmann, G., Winge, D.R., (eds.), Metal Ions in Fungi, Vol. 11 Marcel Dekker, Inc., New York, pp. 39-98.
    • (1994) Metal Ions in Fungi , vol.11 , pp. 39-98
    • van der Helm, D.1    Winkelmann, G.2
  • 25
    • 67651216105 scopus 로고    scopus 로고
    • Siderophore production by marine-derived fungi
    • Holinsworth, B., Martin, J., 2009. Siderophore production by marine-derived fungi. BioMetals 22, 625-632.
    • (2009) BioMetals , vol.22 , pp. 625-632
    • Holinsworth, B.1    Martin, J.2
  • 26
    • 0026717367 scopus 로고
    • Rhizoferrin: a complexone type siderophore of the Mucorales and entomophthorales (Zygomycetes)
    • Thieken, A., Winkelmann, G., 1992. Rhizoferrin: a complexone type siderophore of the Mucorales and entomophthorales (Zygomycetes). FEMS Microbiol. Lett. 73, 37-41.
    • (1992) FEMS Microbiol. Lett. , vol.73 , pp. 37-41
    • Thieken, A.1    Winkelmann, G.2
  • 27
    • 0025851292 scopus 로고
    • The isolation and immunolocalization of iron-binding compounds produced by Gloeophyllum trabeum
    • Jellison, J., Chandhoke, V., Goodell, B., Fekete, F.A., 1991. The isolation and immunolocalization of iron-binding compounds produced by Gloeophyllum trabeum. Appl. Microbiol. Biotechnol. 35, 805-809.
    • (1991) Appl. Microbiol. Biotechnol. , vol.35 , pp. 805-809
    • Jellison, J.1    Chandhoke, V.2    Goodell, B.3    Fekete, F.A.4
  • 28
    • 37249020606 scopus 로고    scopus 로고
    • Citromycetins and bilains A-C: new aromatic polyketides and diketopiperazines from Australian marine-derived and terrestrial Penicillium spp
    • Capon, R.J., Stewart, M., Ratnayake, R., Lacey, E., Gill, J.H., 2007. Citromycetins and bilains A-C: new aromatic polyketides and diketopiperazines from Australian marine-derived and terrestrial Penicillium spp. J. Nat. Prod. 70, 1746-1752.
    • (2007) J. Nat. Prod. , vol.70 , pp. 1746-1752
    • Capon, R.J.1    Stewart, M.2    Ratnayake, R.3    Lacey, E.4    Gill, J.H.5
  • 29
    • 40649120516 scopus 로고    scopus 로고
    • Response to iron deprivation in Saccharomyces cerevisiae
    • Philpott, C.C., Protchenko, O., 2008. Response to iron deprivation in Saccharomyces cerevisiae. Eukaryotic Cell 7, 20-27.
    • (2008) Eukaryotic Cell , vol.7 , pp. 20-27
    • Philpott, C.C.1    Protchenko, O.2
  • 30
    • 0035134461 scopus 로고    scopus 로고
    • Siderophore uptake and use by the yeast Saccharomyces cerevisiae
    • Lesuisse, E., Blaiseau, P-L., Dancis, A., Camadro, J-M., 2001. Siderophore uptake and use by the yeast Saccharomyces cerevisiae. Microbiology 147, 289-298.
    • (2001) Microbiology , vol.147 , pp. 289-298
    • Lesuisse, E.1    Blaiseau, P.-L.2    Dancis, A.3    Camadro, J.-M.4
  • 32
    • 34248649859 scopus 로고    scopus 로고
    • Ecology of siderophores with special reference to the fungi
    • Winkelmann, G., 2007. Ecology of siderophores with special reference to the fungi. BioMetals 20, 379-392.
    • (2007) BioMetals , vol.20 , pp. 379-392
    • Winkelmann, G.1
  • 33
    • 33750622338 scopus 로고    scopus 로고
    • Environmental factors influence the production of enterobactin, salmochelin, aerobactin, and yersiniabactin in Escherichia coli strain nissle 1917
    • Valdebenito, M., Crumbliss, A.L., Winkelmann, G., Hantke, K., 2006. Environmental factors influence the production of enterobactin, salmochelin, aerobactin, and yersiniabactin in Escherichia coli strain nissle 1917. Intern. J. Med Microbiol 296, 513-520.
    • (2006) Intern. J. Med Microbiol , vol.296 , pp. 513-520
    • Valdebenito, M.1    Crumbliss, A.L.2    Winkelmann, G.3    Hantke, K.4
  • 34
    • 0030452653 scopus 로고    scopus 로고
    • A massive phytoplankton bloom induced by an ecosystem-scale iron fertilization experiment in the equatorial Pacific Ocean
    • Coale, K.H., Johnson, K.S., Fitzwater, S.E., Gordon, R.M. et al., 1996. A massive phytoplankton bloom induced by an ecosystem-scale iron fertilization experiment in the equatorial Pacific Ocean. Nature 383, 495-501.
    • (1996) Nature , vol.383 , pp. 495-501
    • Coale, K.H.1    Johnson, K.S.2    Fitzwater, S.E.3    Gordon, R.M.4
  • 35
    • 0034718606 scopus 로고    scopus 로고
    • Microbial iron transport via a siderophore shuttle: a membrane ion transport paradigm
    • Stintzi, A., Barnes, C., Xu, J., Raymond, K.N., 2000. Microbial iron transport via a siderophore shuttle: a membrane ion transport paradigm. Proc. Natl. Acad. Sci. USA 97, 10691-10696.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 10691-10696
    • Stintzi, A.1    Barnes, C.2    Xu, J.3    Raymond, K.N.4
  • 36
    • 3042759136 scopus 로고    scopus 로고
    • Bacterial growth in amniotic fluid is dependent on the iron-availability and the activity of bacterial iron-uptake system
    • Ahn, Y.J., Park, S.K., Oh, J.W., Sun, H.Y., Shin, S.H., 2004. Bacterial growth in amniotic fluid is dependent on the iron-availability and the activity of bacterial iron-uptake system. J. Korean. Med. Sci. 19, 333-340.
    • (2004) J. Korean. Med. Sci. , vol.19 , pp. 333-340
    • Ahn, Y.J.1    Park, S.K.2    Oh, J.W.3    Sun, H.Y.4    Shin, S.H.5
  • 37
    • 79959374583 scopus 로고    scopus 로고
    • Polyphenolic compounds on leaves limit iron availability and affect growth of epiphytic bacteria
    • Karamanoli, K., Bouligaraki, P., Constantinidou, H.I.A., Lindow, S.E., 2011. Polyphenolic compounds on leaves limit iron availability and affect growth of epiphytic bacteria. Ann. App.Biol. 159, 99-108.
    • (2011) Ann. App.Biol. , vol.159 , pp. 99-108
    • Karamanoli, K.1    Bouligaraki, P.2    Constantinidou, H.I.A.3    Lindow, S.E.4
  • 38
    • 0033759220 scopus 로고    scopus 로고
    • Iron metabolism in pathogenic bacteria
    • Ratledge, C., Dover, L.G., 2000. Iron metabolism in pathogenic bacteria. Annu. Rev. Microbiol. 54, 881-941.
    • (2000) Annu. Rev. Microbiol. , vol.54 , pp. 881-941
    • Ratledge, C.1    Dover, L.G.2
  • 40
    • 80053236138 scopus 로고    scopus 로고
    • Molecular mechanisms of Staphylococcus aureus iron acquisition
    • Hammer, N.D., Skaar, E.P., 2011. Molecular mechanisms of Staphylococcus aureus iron acquisition. Annu. Rev. Microbiol. 65, 129-147.
    • (2011) Annu. Rev. Microbiol. , vol.65 , pp. 129-147
    • Hammer, N.D.1    Skaar, E.P.2
  • 41
    • 9244234392 scopus 로고    scopus 로고
    • Bacterial iron sources: from siderophores to hemophores
    • Wandersman, C., Delepelaire, P., 2004. Bacterial iron sources: from siderophores to hemophores. Annu. Rev. Microbiol. 58, 611-647.
    • (2004) Annu. Rev. Microbiol. , vol.58 , pp. 611-647
    • Wandersman, C.1    Delepelaire, P.2
  • 42
    • 84861442326 scopus 로고    scopus 로고
    • Regulating iron storage and metabolism with RNA: an overview of posttranscriptional controls of intracellular iron homeostasis. Wiley Interdisciplinary Reviews: RNA, doi: 10.1002/wrna.102
    • Salvail, H., Massé, E., 2011. Regulating iron storage and metabolism with RNA: an overview of posttranscriptional controls of intracellular iron homeostasis. Wiley Interdisciplinary Reviews: RNA, doi: 10.1002/wrna.102
    • (2011)
    • Salvail, H.1    Massé, E.2
  • 43
    • 0030738431 scopus 로고    scopus 로고
    • Enterobactin biosynthesis in Escherichia coli: isochorismate lyase (EntB) is a bifunctional enzyme that is phosphopantetheinylated by EntD and then acylated by EntE using ATP and 2,3-dihydroxybenzoate
    • Gehring, A.M., Bradley, K.A., Walsh, C.T., 1997. Enterobactin biosynthesis in Escherichia coli: isochorismate lyase (EntB) is a bifunctional enzyme that is phosphopantetheinylated by EntD and then acylated by EntE using ATP and 2, 3-dihydroxybenzoate. Biochemistry 36, 8495-8503.
    • (1997) Biochemistry , vol.36 , pp. 8495-8503
    • Gehring, A.M.1    Bradley, K.A.2    Walsh, C.T.3
  • 44
    • 0033539471 scopus 로고    scopus 로고
    • Assembly of the Pseudomonas aeruginosa nonribosomal peptide siderophore pyochelin: In vitro reconstitution of aryl-4,2-bisthiazoline synthetase activity from PchD, PchE, and PchF
    • Quadri, L.E., Keating, T.A., Patel, H.M., Walsh, C.T., 1999. Assembly of the Pseudomonas aeruginosa nonribosomal peptide siderophore pyochelin: In vitro reconstitution of aryl-4, 2-bisthiazoline synthetase activity from PchD, PchE, and PchF. Biochemistry 38, 14941-14954.
    • (1999) Biochemistry , vol.38 , pp. 14941-14954
    • Quadri, L.E.1    Keating, T.A.2    Patel, H.M.3    Walsh, C.T.4
  • 45
    • 0034687759 scopus 로고    scopus 로고
    • Reconstitution and characterization of the Vibrio cholerae vibriobactin synthetase from VibB, VibE, VibF, and VibH
    • Keating, T.A., Marshall, C.G., Walsh, C.T., 2000. Reconstitution and characterization of the Vibrio cholerae vibriobactin synthetase from VibB, VibE, VibF, and VibH. Biochemistry 39, 15522-15530.
    • (2000) Biochemistry , vol.39 , pp. 15522-15530
    • Keating, T.A.1    Marshall, C.G.2    Walsh, C.T.3
  • 46
    • 0036280341 scopus 로고    scopus 로고
    • Genetics and assembly line enzymology of siderophore biosynthesis in bacteria
    • Crosa, J.H., Walsh, C.T., 2002. Genetics and assembly line enzymology of siderophore biosynthesis in bacteria. Microbiol. Molbiol. Rev. 66, 223-249.
    • (2002) Microbiol. Molbiol. Rev. , vol.66 , pp. 223-249
    • Crosa, J.H.1    Walsh, C.T.2
  • 47
    • 21044449406 scopus 로고    scopus 로고
    • A widely distributed bacterial pathway for siderophore biosynthesis independent of nonribosomal peptide synthetases
    • Challis, G.L., 2005. A widely distributed bacterial pathway for siderophore biosynthesis independent of nonribosomal peptide synthetases. ChembioChem 6, 601-611.
    • (2005) ChembioChem , vol.6 , pp. 601-611
    • Challis, G.L.1
  • 48
    • 70350643410 scopus 로고    scopus 로고
    • The long-overlooked enzymology of a nonribosomal peptide synthetase-independent pathway for virulence-conferring siderophore biosynthesis
    • Oves-Costales, D., Kadi, N., Challis, G.L., 2009. The long-overlooked enzymology of a nonribosomal peptide synthetase-independent pathway for virulence-conferring siderophore biosynthesis. Chem. Commun. 43, 6530-6541.
    • (2009) Chem. Commun. , vol.43 , pp. 6530-6541
    • Oves-Costales, D.1    Kadi, N.2    Challis, G.L.3
  • 49
    • 0029885263 scopus 로고    scopus 로고
    • Novel pyoverdine biosynthesis gene(s) of Pseudomonas aeruginosa PAO
    • Stintzi, A., Cornelis, P., Hohnadel, D., Meyer, J-M. et al., 1996. Novel pyoverdine biosynthesis gene(s) of Pseudomonas aeruginosa PAO. Microbiology 142, 1181-1190.
    • (1996) Microbiology , vol.142 , pp. 1181-1190
    • Stintzi, A.1    Cornelis, P.2    Hohnadel, D.3    Meyer, J.-M.4
  • 50
    • 18644368300 scopus 로고    scopus 로고
    • Identification of new, conserved, non-ribosomal peptide synthetases from fluorescent pseudomonads involved in the biosynthesis of the siderophore pyoverdine
    • Mossialos, D., Ochsner, U., Baysse, C., Chablain, P. et al., 2002. Identification of new, conserved, non-ribosomal peptide synthetases from fluorescent pseudomonads involved in the biosynthesis of the siderophore pyoverdine. Mol. Microbiol. 45, 1673-1685.
    • (2002) Mol. Microbiol. , vol.45 , pp. 1673-1685
    • Mossialos, D.1    Ochsner, U.2    Baysse, C.3    Chablain, P.4
  • 51
    • 33645979649 scopus 로고    scopus 로고
    • Characterization of a gene encoding an acetylase required for pyoverdine synthesis in Pseudomonas aeruginosa
    • Lamont, I.L., Martin, L.W., Sims, T., Scott, A., Wallace, M., 2006. Characterization of a gene encoding an acetylase required for pyoverdine synthesis in Pseudomonas aeruginosa. J. Bacteriol. 188, 3149-3152.
    • (2006) J. Bacteriol. , vol.188 , pp. 3149-3152
    • Lamont, I.L.1    Martin, L.W.2    Sims, T.3    Scott, A.4    Wallace, M.5
  • 52
    • 0032211974 scopus 로고    scopus 로고
    • Identification of a Mycobacterium tuberculosis gene cluster encoding the biosynthetic enzymes for assembly of the virulence-conferring siderophore mycobactin
    • Quadri, L.E.N., Sello, J., Keating, T.A., Weinreb, P.H., Walsh, C.T., 1998. Identification of a Mycobacterium tuberculosis gene cluster encoding the biosynthetic enzymes for assembly of the virulence-conferring siderophore mycobactin. Chem. Biol. 5, 631-645.
    • (1998) Chem. Biol. , vol.5 , pp. 631-645
    • Quadri, L.E.N.1    Sello, J.2    Keating, T.A.3    Weinreb, P.H.4    Walsh, C.T.5
  • 53
    • 33645116726 scopus 로고    scopus 로고
    • Chemoenzymatic and template-directed synthesis of bioactive macrocyclic peptides
    • Grünewald, J., Marahiel, M.A., 2006. Chemoenzymatic and template-directed synthesis of bioactive macrocyclic peptides. Microbiol. Mol. Biol. R. 70, 121-146.
    • (2006) Microbiol. Mol. Biol. R. , vol.70 , pp. 121-146
    • Grünewald, J.1    Marahiel, M.A.2
  • 54
    • 9244234513 scopus 로고    scopus 로고
    • Biosynthesis of nonribosomal peptides
    • Finking, R., Marahiel, M.A., 2004. Biosynthesis of nonribosomal peptides. Annu. Rev. Microbiol. 58, 453-488.
    • (2004) Annu. Rev. Microbiol. , vol.58 , pp. 453-488
    • Finking, R.1    Marahiel, M.A.2
  • 55
    • 0035912883 scopus 로고    scopus 로고
    • Generality of peptide cyclization catalyzed by isolated thioesterase domains of nonribosomal peptide synthetases
    • Kohli, R.M., Trauger, J.W., Schwarzer, D., Marahiel, M.A., Walsh, C.T., 2001. Generality of peptide cyclization catalyzed by isolated thioesterase domains of nonribosomal peptide synthetases. Biochemistry 40, 7099-7108.
    • (2001) Biochemistry , vol.40 , pp. 7099-7108
    • Kohli, R.M.1    Trauger, J.W.2    Schwarzer, D.3    Marahiel, M.A.4    Walsh, C.T.5
  • 56
    • 0034646227 scopus 로고    scopus 로고
    • The Entf and Ente adenylation domains of Escherichia coli enterobactin synthetase: Sequestration and selectivity in acyl-amp transfers to thiolation domain cosubstrates
    • Ehmann, D.E., Shaw-Reid, C.A., Losey, H.C., Walsh, C.T., 2000. The Entf and Ente adenylation domains of Escherichia coli enterobactin synthetase: Sequestration and selectivity in acyl-amp transfers to thiolation domain cosubstrates. Proc. Nat. Acad. Sci. 97, 2509-2514.
    • (2000) Proc. Nat. Acad. Sci. , vol.97 , pp. 2509-2514
    • Ehmann, D.E.1    Shaw-Reid, C.A.2    Losey, H.C.3    Walsh, C.T.4
  • 57
    • 33947394461 scopus 로고    scopus 로고
    • Biosynthetic analysis of the petrobactin siderophore pathway from Bacillus anthracis
    • Lee, J.Y., Janes, B.K., Passalacqua, K.D., Pfleger, B.F. et al., 2007. Biosynthetic analysis of the petrobactin siderophore pathway from Bacillus anthracis. J. Bacteriol. 189, 1698-1710.
    • (2007) J. Bacteriol. , vol.189 , pp. 1698-1710
    • Lee, J.Y.1    Janes, B.K.2    Passalacqua, K.D.3    Pfleger, B.F.4
  • 58
    • 0028847512 scopus 로고
    • Identification of alcaligin as the siderophore produced by Bordetella pertussis and B. bronchiseptica
    • Moore, C.H., Foster, L.A., Gerbig, D.G., Dyer, D.W., Gibson, B.W., 1995. Identification of alcaligin as the siderophore produced by Bordetella pertussis and B. bronchiseptica. J. Bacteriol. 177, 1116-1118.
    • (1995) J. Bacteriol. , vol.177 , pp. 1116-1118
    • Moore, C.H.1    Foster, L.A.2    Gerbig, D.G.3    Dyer, D.W.4    Gibson, B.W.5
  • 59
    • 79959389446 scopus 로고    scopus 로고
    • Iron uptake systems in pathogenic Bordetella
    • Cornelis, P., Andrews, S.C., eds., Caiste Academic Press, Norfolk, UK.
    • Brickman, T.J., Armstrong, S.K., 2010. Iron uptake systems in pathogenic Bordetella. In: Cornelis, P., Andrews, S.C., (eds.), Iron Uptake and Homeostasis in Microorganisms. Caiste Academic Press, Norfolk, UK.
    • (2010) Iron Uptake and Homeostasis in Microorganisms
    • Brickman, T.J.1    Armstrong, S.K.2
  • 60
    • 61449173810 scopus 로고    scopus 로고
    • Identification and characterization of the Staphylococcus aureus gene cluster coding for staphyloferrin A
    • Cotton, J.L., Tao, J., Balibar, C.J., 2009. Identification and characterization of the Staphylococcus aureus gene cluster coding for staphyloferrin A. Biochemistry 48, 1025-1035.
    • (2009) Biochemistry , vol.48 , pp. 1025-1035
    • Cotton, J.L.1    Tao, J.2    Balibar, C.J.3
  • 61
    • 0023258960 scopus 로고
    • Operator sequences of the aerobactin operon of plasmid ColV-K30 binding the ferric uptake regulation (fur) repressor
    • De Lorenzo, V., Wee, S., Herrero, M., Neilands, J.B., 1987. Operator sequences of the aerobactin operon of plasmid ColV-K30 binding the ferric uptake regulation (fur) repressor. J. Bacteriol. 169, 2624-2630.
    • (1987) J. Bacteriol. , vol.169 , pp. 2624-2630
    • De Lorenzo, V.1    Wee, S.2    Herrero, M.3    Neilands, J.B.4
  • 62
    • 0031850630 scopus 로고    scopus 로고
    • Bacillus subtilis contains multiple Fur homologues: identification of the iron uptake (Fur) and peroxide regulon (PerR) repressors
    • Bsat, N., Herbig, A., Casillas-Martinez, L., Setlow, P., Helmann, J.D., 1998. Bacillus subtilis contains multiple Fur homologues: identification of the iron uptake (Fur) and peroxide regulon (PerR) repressors. Mol. Microbiol. 29, 189-198.
    • (1998) Mol. Microbiol. , vol.29 , pp. 189-198
    • Bsat, N.1    Herbig, A.2    Casillas-Martinez, L.3    Setlow, P.4    Helmann, J.D.5
  • 63
    • 0034113354 scopus 로고    scopus 로고
    • Molecular characterization of the ferric-uptake regulator, Fur, from Staphylococcus aureus
    • Xiong, A., Singh, V.K., Cabrera, G., Jayaswal, R.K., 2000. Molecular characterization of the ferric-uptake regulator, Fur, from Staphylococcus aureus. Microbiology 146, 659-668.
    • (2000) Microbiology , vol.146 , pp. 659-668
    • Xiong, A.1    Singh, V.K.2    Cabrera, G.3    Jayaswal, R.K.4
  • 66
    • 34248669844 scopus 로고    scopus 로고
    • How we learnt about iron acquisition in Pseudomonas aeruginosa: a series of very fortunate events
    • Vasil, M., 2007. How we learnt about iron acquisition in Pseudomonas aeruginosa: a series of very fortunate events. BioMetals 20, 587-601.
    • (2007) BioMetals , vol.20 , pp. 587-601
    • Vasil, M.1
  • 67
    • 79961063576 scopus 로고    scopus 로고
    • Mapping the regulon of Vibrio cholerae ferric uptake regulator expands its known network of gene regulation
    • Davies, B.W., Bogard, R.W., Mekalanos, J.J., 2011. Mapping the regulon of Vibrio cholerae ferric uptake regulator expands its known network of gene regulation. Proc. Natl. Acad. Sci. 108, 12467-12472.
    • (2011) Proc. Natl. Acad. Sci. , vol.108 , pp. 12467-12472
    • Davies, B.W.1    Bogard, R.W.2    Mekalanos, J.J.3
  • 68
    • 41949127541 scopus 로고    scopus 로고
    • The iron-responsive Fur regulon in Yersinia pestis
    • Gao, H., Zhou, D., Li, Y., Guo, Z. et al., 2008. The iron-responsive Fur regulon in Yersinia pestis. J. Bacteriol. 190, 3063-3075.
    • (2008) J. Bacteriol. , vol.190 , pp. 3063-3075
    • Gao, H.1    Zhou, D.2    Li, Y.3    Guo, Z.4
  • 69
    • 0035069457 scopus 로고    scopus 로고
    • Iron and metal regulation in bacteria
    • Hantke, K., 2001. Iron and metal regulation in bacteria. Curr. Opin. Microbiol. 4, 172-177.
    • (2001) Curr. Opin. Microbiol. , vol.4 , pp. 172-177
    • Hantke, K.1
  • 70
    • 0033954445 scopus 로고    scopus 로고
    • Surface signaling in ferric citrate transport gene induction: interaction of the FecA, FecR, and FecI regulatory proteins
    • Enz, S., Mahren, S., Stroeher, U.H., Braun, V., 2000. Surface signaling in ferric citrate transport gene induction: interaction of the FecA, FecR, and FecI regulatory proteins. J. Bacteriol. 182, 637-646.
    • (2000) J. Bacteriol. , vol.182 , pp. 637-646
    • Enz, S.1    Mahren, S.2    Stroeher, U.H.3    Braun, V.4
  • 71
    • 23744444687 scopus 로고    scopus 로고
    • Transmembrane transcriptional control (surface signalling) of the Escherichia coli Fec type
    • Braun, V., Mahren, S., 2005. Transmembrane transcriptional control (surface signalling) of the Escherichia coli Fec type. FEMS Microbiol. Rev. 29, 673-684.
    • (2005) FEMS Microbiol. Rev. , vol.29 , pp. 673-684
    • Braun, V.1    Mahren, S.2
  • 72
    • 0037221477 scopus 로고    scopus 로고
    • Siderophore-mediated cell signalling in Pseudomonas aeruginosa: divergent pathways regulate virulence factor production and siderophore receptor synthesis
    • Beare, P.A., For, R.J., Martin, L.W., Lamont, I.L., 2003. Siderophore-mediated cell signalling in Pseudomonas aeruginosa: divergent pathways regulate virulence factor production and siderophore receptor synthesis. Mol. Microbiol. 47, 195-207.
    • (2003) Mol. Microbiol. , vol.47 , pp. 195-207
    • Beare, P.A.1    For, R.J.2    Martin, L.W.3    Lamont, I.L.4
  • 73
    • 23644456000 scopus 로고    scopus 로고
    • FpvIR control of fpvA ferric pyoverdine receptor gene expression in Pseudomonas aeruginosa: Demonstration of an interaction between FpvI and FpvR and identification of mutations in each compromising this interaction
    • Rédly, G.A., Poole, K., 2005. FpvIR control of fpvA ferric pyoverdine receptor gene expression in Pseudomonas aeruginosa: Demonstration of an interaction between FpvI and FpvR and identification of mutations in each compromising this interaction. J. Bacteriol. 187, 5648-5657.
    • (2005) J. Bacteriol. , vol.187 , pp. 5648-5657
    • Rédly, G.A.1    Poole, K.2
  • 74
    • 70450216072 scopus 로고    scopus 로고
    • Different roles for anti-sigma factors in siderophore signalling pathways of Pseudomonas aeruginosa
    • Mettrick, K.A., Lamont, I.L., 2009. Different roles for anti-sigma factors in siderophore signalling pathways of Pseudomonas aeruginosa. Mol. Microbiol. 74, 1257-1271.
    • (2009) Mol. Microbiol. , vol.74 , pp. 1257-1271
    • Mettrick, K.A.1    Lamont, I.L.2
  • 75
    • 0029787967 scopus 로고    scopus 로고
    • PfeR, an enterobactin-responsive activator of ferric enterobactin receptor gene expression in Pseudomonas aeruginosa
    • Dean, C.R., Neshat, S., Poole, K., 1996. PfeR, an enterobactin-responsive activator of ferric enterobactin receptor gene expression in Pseudomonas aeruginosa. J. Bacteriol. 178, 5361-5369.
    • (1996) J. Bacteriol. , vol.178 , pp. 5361-5369
    • Dean, C.R.1    Neshat, S.2    Poole, K.3
  • 76
    • 33748675699 scopus 로고    scopus 로고
    • The Bordetella Bfe sSystem: gGrowth and transcriptional response to siderophores, catechols, and neuroendocrine catecholamines
    • Anderson, M.T., Armstrong, S.K., 2006. The Bordetella Bfe sSystem: gGrowth and transcriptional response to siderophores, catechols, and neuroendocrine catecholamines. J. Bacteriol. 188, 5731-5740.
    • (2006) J. Bacteriol. , vol.188 , pp. 5731-5740
    • Anderson, M.T.1    Armstrong, S.K.2
  • 77
    • 77953222872 scopus 로고    scopus 로고
    • Stereospecific recognition of pyochelin and enantio-pyochelin by the PchR proteins in fluorescent pseudomonads
    • Youard, Z.A., Reimmann, C., 2010. Stereospecific recognition of pyochelin and enantio-pyochelin by the PchR proteins in fluorescent pseudomonads. Microbiol. 156, 1772-1782.
    • (2010) Microbiol. , vol.156 , pp. 1772-1782
    • Youard, Z.A.1    Reimmann, C.2
  • 78
    • 33751006455 scopus 로고    scopus 로고
    • Transcriptional regulation of the pdt gene cluster of Pseudomonas stutzeri KC involves an AraC/XylS family transcriptional activator (PdtC) and the cognate siderophore Pyridine-2,6-Bis(Thiocarboxylic Acid)
    • Morales, S.E., Lewis, T.A., 2006. Transcriptional regulation of the pdt gene cluster of Pseudomonas stutzeri KC involves an AraC/XylS family transcriptional activator (PdtC) and the cognate siderophore Pyridine-2, 6-Bis(Thiocarboxylic Acid). Appl. Environ. Microbiol. 72, 6994-7002.
    • (2006) Appl. Environ. Microbiol. , vol.72 , pp. 6994-7002
    • Morales, S.E.1    Lewis, T.A.2
  • 79
    • 79961061063 scopus 로고    scopus 로고
    • Identification of the in vitro target of an iron-responsive AraC-like protein from Neisseria meningitidis that is in a regulatory cascade with Fur
    • Fantappiè, L., Scarlato, V., Delany, I., 2011. Identification of the in vitro target of an iron-responsive AraC-like protein from Neisseria meningitidis that is in a regulatory cascade with Fur. Microbiology 157, 2235-2247.
    • (2011) Microbiology , vol.157 , pp. 2235-2247
    • Fantappiè, L.1    Scarlato, V.2    Delany, I.3
  • 80
    • 0029806389 scopus 로고    scopus 로고
    • YbtA, an AraC-type regulator of the Yersinia pestis pesticin/yersiniabactin receptor
    • Fetherston, J.D., Bearden, S.W., Perry, R.D., 1996. YbtA, an AraC-type regulator of the Yersinia pestis pesticin/yersiniabactin receptor. Mol. Microbiol. 22, 315-325.
    • (1996) Mol. Microbiol. , vol.22 , pp. 315-325
    • Fetherston, J.D.1    Bearden, S.W.2    Perry, R.D.3
  • 81
    • 77951242175 scopus 로고    scopus 로고
    • The yersiniabactin transports system is critical for the pathogenesis of bubonic and pneumonic Plague
    • Fetherston, J.D., Kirillina, O., Bobrov, A.G., Paulley, J.T., Perry, R.D., 2010. The yersiniabactin transports system is critical for the pathogenesis of bubonic and pneumonic Plague. Infect. Immun. 78, 2045-2052.
    • (2010) Infect. Immun. , vol.78 , pp. 2045-2052
    • Fetherston, J.D.1    Kirillina, O.2    Bobrov, A.G.3    Paulley, J.T.4    Perry, R.D.5
  • 82
    • 0035156057 scopus 로고    scopus 로고
    • Transcriptional activation of Bordetella alcaligin siderophore genes requires the AlcR regulator with alcaligin as inducer
    • Brickman, T.J., Kang, H.Y., Armstrong, S.K., 2001. Transcriptional activation of Bordetella alcaligin siderophore genes requires the AlcR regulator with alcaligin as inducer. J. Bacteriol. 183, 483.
    • (2001) J. Bacteriol. , vol.183 , pp. 483
    • Brickman, T.J.1    Kang, H.Y.2    Armstrong, S.K.3
  • 83
    • 0026099665 scopus 로고
    • Positive transcriptional regulation of an iron-regulated virulence gene in Vibrio cholerae
    • Goldberg, M.B., Boyko, S.A., Calderwood, S.B., 1991. Positive transcriptional regulation of an iron-regulated virulence gene in Vibrio cholerae. Proc. Natl. Acad. Sci. 88, 1125-1129.
    • (1991) Proc. Natl. Acad. Sci. , vol.88 , pp. 1125-1129
    • Goldberg, M.B.1    Boyko, S.A.2    Calderwood, S.B.3
  • 84
    • 84886768156 scopus 로고    scopus 로고
    • Identification and characterization of a novel outer membrane protein receptor FetA for ferric enterobactin transport in Vibrio anguillarum 775 (pJM1)
    • Naka, H., Crosa, J.H., 2011. Identification and characterization of a novel outer membrane protein receptor FetA for ferric enterobactin transport in Vibrio anguillarum 775 (pJM1). BioMetals 1-9.
    • (2011) BioMetals , pp. 1-9
    • Naka, H.1    Crosa, J.H.2
  • 85
    • 2942748428 scopus 로고    scopus 로고
    • The binding mechanism of pyoverdine with the outer membrane receptor FpvA in Pseudomonas aeruginosa is dependent on its iron-loaded status
    • Clément, E., Mesini, P.J., Pattus, F., Schalk, I.J., 2004. The binding mechanism of pyoverdine with the outer membrane receptor FpvA in Pseudomonas aeruginosa is dependent on its iron-loaded status. Biochemistry 43, 7954-7965.
    • (2004) Biochemistry , vol.43 , pp. 7954-7965
    • Clément, E.1    Mesini, P.J.2    Pattus, F.3    Schalk, I.J.4
  • 86
    • 0025087690 scopus 로고
    • Pyoverdine-facilitated iron uptake in Pseudomonas aeruginosa: immunological characterization of the ferripyoverdine receptor
    • Meyer, J.M., Hohnadel, D., Khan, A., Cornelis, P., 1990. Pyoverdine-facilitated iron uptake in Pseudomonas aeruginosa: immunological characterization of the ferripyoverdine receptor. Mol. Microbiol. 4, 1401-1405.
    • (1990) Mol. Microbiol. , vol.4 , pp. 1401-1405
    • Meyer, J.M.1    Hohnadel, D.2    Khan, A.3    Cornelis, P.4
  • 87
    • 0027367171 scopus 로고
    • Cloning and sequence analysis of an EnvCD homologue in Pseudomonas aeruginosa: regulation by iron and possible involvement in the secretion of the siderophore pyoverdine
    • Poole, K., Heinrichs, D.E., Neshat, S., 1993. Cloning and sequence analysis of an EnvCD homologue in Pseudomonas aeruginosa: regulation by iron and possible involvement in the secretion of the siderophore pyoverdine. Mol. Microbiol. 10, 529-544.
    • (1993) Mol. Microbiol. , vol.10 , pp. 529-544
    • Poole, K.1    Heinrichs, D.E.2    Neshat, S.3
  • 88
    • 0037312849 scopus 로고    scopus 로고
    • Pyoverdine-mediated regulation of FpvA synthesis in Pseudomonas aeruginosa: involvement of a probable extracytoplasmic-function sigma factor
    • Rédly, G.A., Poole, K., 2003. Pyoverdine-mediated regulation of FpvA synthesis in Pseudomonas aeruginosa: involvement of a probable extracytoplasmic-function sigma factor, FpvI.J. Bacteriol. 185, 1261-1265.
    • (2003) FpvI.J. Bacteriol. , vol.185 , pp. 1261-1265
    • Rédly, G.A.1    Poole, K.2
  • 89
    • 0036271269 scopus 로고    scopus 로고
    • FpvA receptor involvement in pyoverdine biosynthesis in Pseudomonas aeruginosa
    • Shen, J., Meldrum, A., Poole, K., 2002. FpvA receptor involvement in pyoverdine biosynthesis in Pseudomonas aeruginosa. J. Bacteriol. 184, 3268-3275.
    • (2002) J. Bacteriol. , vol.184 , pp. 3268-3275
    • Shen, J.1    Meldrum, A.2    Poole, K.3
  • 90
    • 0038076005 scopus 로고    scopus 로고
    • Identification and characterization of novel pyoverdine synthesis genes in Pseudomonas aeruginosa
    • Lamont, I.L., Martin, L.W., 2003. Identification and characterization of novel pyoverdine synthesis genes in Pseudomonas aeruginosa. Microbiology 149, 833-842.
    • (2003) Microbiology , vol.149 , pp. 833-842
    • Lamont, I.L.1    Martin, L.W.2
  • 91
    • 0029015364 scopus 로고
    • Cloning and characterization of pvdS, a gene required for pyoverdine synthesis in Pseudomonas aeruginosa: PvdS is probably an alternative sigma factor
    • Cunliffe, H.E., Merriman, T.R., Lamont, I.L., 1995. Cloning and characterization of pvdS, a gene required for pyoverdine synthesis in Pseudomonas aeruginosa: PvdS is probably an alternative sigma factor. J. Bacteriol. 177, 2744-2750.
    • (1995) J. Bacteriol. , vol.177 , pp. 2744-2750
    • Cunliffe, H.E.1    Merriman, T.R.2    Lamont, I.L.3
  • 92
    • 0035982906 scopus 로고    scopus 로고
    • GeneChip® expression analysis of the iron starvation response in Pseudomonas aeruginosa: identification of novel pyoverdine biosynthesis genes
    • Ochsner, U.A., Wilderman, P.J., Vasil, A.I., Vasil, M.L., 2002. GeneChip® expression analysis of the iron starvation response in Pseudomonas aeruginosa: identification of novel pyoverdine biosynthesis genes. Mol. Microbiol. 45, 1277-1287.
    • (2002) Mol. Microbiol. , vol.45 , pp. 1277-1287
    • Ochsner, U.A.1    Wilderman, P.J.2    Vasil, A.I.3    Vasil, M.L.4
  • 93
    • 0036772656 scopus 로고    scopus 로고
    • The Pseudomonas aeruginosa alternative sigma factor PvdS controls exotoxin A expression and is expressed in lung infections associated with cystic fibrosis
    • Hunt, T.A., Peng, W-T., Loubens, I., Storey, D.G., 2002. The Pseudomonas aeruginosa alternative sigma factor PvdS controls exotoxin A expression and is expressed in lung infections associated with cystic fibrosis. Microbiology 148, 3183-3193.
    • (2002) Microbiology , vol.148 , pp. 3183-3193
    • Hunt, T.A.1    Peng, W.-T.2    Loubens, I.3    Storey, D.G.4
  • 94
    • 0034873465 scopus 로고    scopus 로고
    • Characterization of an endoprotease (PrpL) encoded by a PvdS-regulated gene in Pseudomonas aeruginosa
    • Wilderman, P.J., Vasil, A.I., Johnson, Z., Wilson, M.J. et al., 2001. Characterization of an endoprotease (PrpL) encoded by a PvdS-regulated gene in Pseudomonas aeruginosa. Infect. Immun. 69, 5385-5394.
    • (2001) Infect. Immun. , vol.69 , pp. 5385-5394
    • Wilderman, P.J.1    Vasil, A.I.2    Johnson, Z.3    Wilson, M.J.4
  • 95
    • 33845951159 scopus 로고    scopus 로고
    • Interactions between TonB from Escherichia coli and the periplasmic protein FhuD
    • Carter, D.M., Miousse, I.R., Gagnon, J-N., Martinez, É. et al., 2006. Interactions between TonB from Escherichia coli and the periplasmic protein FhuD. J. Biol. Chem. 281, 35413-35424.
    • (2006) J. Biol. Chem. , vol.281 , pp. 35413-35424
    • Carter, D.M.1    Miousse, I.R.2    Gagnon, J.-N.3    Martinez, É.4
  • 96
    • 28844479346 scopus 로고    scopus 로고
    • FpvA-mediated ferric pyoverdine uptake in Pseudomonas aeruginosa: identification of aromatic residues in FpvA implicated in ferric pyoverdine binding and transport
    • Shen, J-S., Geoffroy, V., Neshat, S., Jia, Z. et al., 2005. FpvA-mediated ferric pyoverdine uptake in Pseudomonas aeruginosa: identification of aromatic residues in FpvA implicated in ferric pyoverdine binding and transport. J. Bacteriol. 187, 8511-8515.
    • (2005) J. Bacteriol. , vol.187 , pp. 8511-8515
    • Shen, J.-S.1    Geoffroy, V.2    Neshat, S.3    Jia, Z.4
  • 97
    • 0036015639 scopus 로고    scopus 로고
    • Export of the siderophore enterobactin in Escherichia coli: involvement of a 43kDa membrane exporter
    • Furrer, J.L., Sanders, D.N., Hook-Barnard, I.G., Mcintosh, M.A., 2002. Export of the siderophore enterobactin in Escherichia coli: involvement of a 43kDa membrane exporter. Mol. Microbiol. 44, 1225-1234.
    • (2002) Mol. Microbiol. , vol.44 , pp. 1225-1234
    • Furrer, J.L.1    Sanders, D.N.2    Hook-Barnard, I.G.3    Mcintosh, M.A.4
  • 98
    • 25144462979 scopus 로고    scopus 로고
    • TolC is involved in enterobactin efflux across the outer membrane of Escherichia coli
    • Bleuel, C., Große, C., Taudte, N., Scherer, J. et al., 2005. TolC is involved in enterobactin efflux across the outer membrane of Escherichia coli. J. Bacteriol. 187, 6701-6707.
    • (2005) J. Bacteriol. , vol.187 , pp. 6701-6707
    • Bleuel, C.1    Große, C.2    Taudte, N.3    Scherer, J.4
  • 99
    • 48149100258 scopus 로고    scopus 로고
    • The major facilitator superfamily-type transporter YmfE and the multidrug-efflux activator Mta mediate bacillibactin secretion in Bacillus subtilis
    • Miethke, M., Schmidt, S., Marahiel, M.A., 2008. The major facilitator superfamily-type transporter YmfE and the multidrug-efflux activator Mta mediate bacillibactin secretion in Bacillus subtilis. J. Bacteriol. 190, 5143-5152.
    • (2008) J. Bacteriol. , vol.190 , pp. 5143-5152
    • Miethke, M.1    Schmidt, S.2    Marahiel, M.A.3
  • 100
    • 0027203781 scopus 로고
    • Cloning and nucleotide sequence analysis of the ferripyoverdine receptor gene fpvA of Pseudomonas aeruginosa
    • Poole, K., Neshat, S., Krebes, K., Heinrichs, D.E., 1993. Cloning and nucleotide sequence analysis of the ferripyoverdine receptor gene fpvA of Pseudomonas aeruginosa. J. Bacteriol. 175, 4597-4604.
    • (1993) J. Bacteriol. , vol.175 , pp. 4597-4604
    • Poole, K.1    Neshat, S.2    Krebes, K.3    Heinrichs, D.E.4
  • 101
    • 66149134410 scopus 로고    scopus 로고
    • Efflux unbalance in Pseudomonas aeruginosa isolates from cystic fibrosis patients
    • Vettoretti, L., Plésiat, P., Muller, C., El Garch, F. et al., 2009. Efflux unbalance in Pseudomonas aeruginosa isolates from cystic fibrosis patients. Antimicrob. Agents Chemother. 53, 1987-1997.
    • (2009) Antimicrob. Agents Chemother. , vol.53 , pp. 1987-1997
    • Vettoretti, L.1    Plésiat, P.2    Muller, C.3    El Garch, F.4
  • 102
    • 79959448572 scopus 로고    scopus 로고
    • Staphylococcus aureus transporters Hts, Sir, and Sst capture iron liberated from human transferrin by staphyloferrin A, staphyloferrin B, and catecholamine stress hormones, respectively, and contribute to virulence
    • Beasley, F.C., Marolda, C.L., Cheung, J., Buac, S., Heinrichs, D.E., 2011. Staphylococcus aureus transporters Hts, Sir, and Sst capture iron liberated from human transferrin by staphyloferrin A, staphyloferrin B, and catecholamine stress hormones, respectively, and contribute to virulence. Infect. Immun. 79, 2345-2355.
    • (2011) Infect. Immun. , vol.79 , pp. 2345-2355
    • Beasley, F.C.1    Marolda, C.L.2    Cheung, J.3    Buac, S.4    Heinrichs, D.E.5
  • 103
    • 77951234543 scopus 로고    scopus 로고
    • The Staphylococcus aureus siderophore receptor HtsA undergoes localized conformational changes to enclose staphyloferrin A in an arginine-rich binding pocket
    • Grigg, J.C., Cooper, J.D., Cheung, J., Heinrichs, D.E., Murphy, M.E.P., 2010. The Staphylococcus aureus siderophore receptor HtsA undergoes localized conformational changes to enclose staphyloferrin A in an arginine-rich binding pocket. J. Biol. Chem. 285, 11162-11171.
    • (2010) J. Biol. Chem. , vol.285 , pp. 11162-11171
    • Grigg, J.C.1    Cooper, J.D.2    Cheung, J.3    Heinrichs, D.E.4    Murphy, M.E.P.5
  • 104
    • 30744441922 scopus 로고    scopus 로고
    • Identification of an ABC transporter required for iron acquisition and virulence in Mycobacterium tuberculosis
    • Rodriguez, G.M., Smith, I., 2006. Identification of an ABC transporter required for iron acquisition and virulence in Mycobacterium tuberculosis. J. Bacteriol. 188, 424-430.
    • (2006) J. Bacteriol. , vol.188 , pp. 424-430
    • Rodriguez, G.M.1    Smith, I.2
  • 105
    • 47749094684 scopus 로고    scopus 로고
    • Mechanistic insights into a novel exporter-importer system of Mycobacterium tuberculosis unravel its role in trafficking of iron
    • Farhana, A., Kumar, S., Rathore, S.S., Ghosh, P.C. et al., 2008. Mechanistic insights into a novel exporter-importer system of Mycobacterium tuberculosis unravel its role in trafficking of iron. PLoS One 3, e2087.
    • (2008) PLoS One , vol.3
    • Farhana, A.1    Kumar, S.2    Rathore, S.S.3    Ghosh, P.C.4
  • 106
    • 34047268399 scopus 로고    scopus 로고
    • Real time fluorescent resonance energy transfer visualization of ferric pyoverdine uptake in Pseudomonas aeruginosa
    • Greenwald, J., Hoegy, F., Nader, M., Journet, L. et al., 2007. Real time fluorescent resonance energy transfer visualization of ferric pyoverdine uptake in Pseudomonas aeruginosa. J Biol Chem 282, 2987-2995.
    • (2007) J Biol Chem , vol.282 , pp. 2987-2995
    • Greenwald, J.1    Hoegy, F.2    Nader, M.3    Journet, L.4
  • 107
    • 78649645704 scopus 로고    scopus 로고
    • An efflux pump is required for siderophore recycling by Pseudomonas aeruginosa
    • Yeterian, E., Martin, L.W., Lamont, I.L., Schalk, I.J., 2010. An efflux pump is required for siderophore recycling by Pseudomonas aeruginosa. Environm. Microbiol. Reports 2, 412-418.
    • (2010) Environm. Microbiol. Reports , vol.2 , pp. 412-418
    • Yeterian, E.1    Martin, L.W.2    Lamont, I.L.3    Schalk, I.J.4
  • 108
    • 77749270483 scopus 로고    scopus 로고
    • The ferrichrome uptake pathway in Pseudomonas aeruginosa involves an iron release mechanism with acylation of the siderophore and recycling of the modified desferrichrome
    • Hannauer, M., Barda, Y., Mislin, G.L.A., Shanzer, A., Schalk, I.J., 2010. The ferrichrome uptake pathway in Pseudomonas aeruginosa involves an iron release mechanism with acylation of the siderophore and recycling of the modified desferrichrome. J. Bacteriol. 192, 1212-1220.
    • (2010) J. Bacteriol. , vol.192 , pp. 1212-1220
    • Hannauer, M.1    Barda, Y.2    Mislin, G.L.A.3    Shanzer, A.4    Schalk, I.J.5
  • 109
    • 0024675811 scopus 로고
    • Iron-hydroxamate transport into Escherichia coli K12: Localization of FhuD in the periplasm and of FhuB in the cytoplasmic membrane
    • Köster, W., Braun, V., 1989. Iron-hydroxamate transport into Escherichia coli K12: Localization of FhuD in the periplasm and of FhuB in the cytoplasmic membrane. Mol. Gen. Genetics 217, 233-239.
    • (1989) Mol. Gen. Genetics , vol.217 , pp. 233-239
    • Köster, W.1    Braun, V.2
  • 110
    • 73949146114 scopus 로고    scopus 로고
    • Molecular basis of pyoverdine siderophore recycling in Pseudomonas aeruginosa
    • Imperi, F., Tiburzi, F., Visca, P., 2009. Molecular basis of pyoverdine siderophore recycling in Pseudomonas aeruginosa. Proc. Natl. Acad. Sci. 106, 20440-20445.
    • (2009) Proc. Natl. Acad. Sci. , vol.106 , pp. 20440-20445
    • Imperi, F.1    Tiburzi, F.2    Visca, P.3
  • 111
    • 0037010152 scopus 로고    scopus 로고
    • Iron transport and signaling in Escherichia coli
    • Braun, V., Braun, M., 2002. Iron transport and signaling in Escherichia coli. FEBS Lett. 529, 78-85.
    • (2002) FEBS Lett. , vol.529 , pp. 78-85
    • Braun, V.1    Braun, M.2
  • 112
    • 34248634581 scopus 로고    scopus 로고
    • Molecular mechanism of ferric siderophore passage through the outer membrane receptor proteins of Escherichia coli
    • Chakraborty, R., Storey, E., Van Der Helm, D., 2007. Molecular mechanism of ferric siderophore passage through the outer membrane receptor proteins of Escherichia coli. BioMetals 20, 263-274.
    • (2007) BioMetals , vol.20 , pp. 263-274
    • Chakraborty, R.1    Storey, E.2    Van Der Helm, D.3
  • 113
    • 33846948630 scopus 로고    scopus 로고
    • Evidence of ball-and-chain transport of ferric enterobactin through FepA
    • Ma, L., Kaserer, W., Annamalai, R., Scott, D.C. et al., 2007. Evidence of ball-and-chain transport of ferric enterobactin through FepA. J. Biol. Chem. 282, 397-406.
    • (2007) J. Biol. Chem. , vol.282 , pp. 397-406
    • Ma, L.1    Kaserer, W.2    Annamalai, R.3    Scott, D.C.4
  • 114
    • 53849140416 scopus 로고    scopus 로고
    • The metal dependence of pyoverdine interactions with its outer membrane receptor FpvA
    • Greenwald, J., Zeder-Lutz, G., Hagege, A., Celia, H., Pattus, F., 2008. The metal dependence of pyoverdine interactions with its outer membrane receptor FpvA. J. Bacteriol. 190, 6548-6558.
    • (2008) J. Bacteriol. , vol.190 , pp. 6548-6558
    • Greenwald, J.1    Zeder-Lutz, G.2    Hagege, A.3    Celia, H.4    Pattus, F.5
  • 115
    • 79953183933 scopus 로고    scopus 로고
    • Mechanism of ferripyoverdine uptake by Pseudomonas aeruginosa outer membrane transporter FpvA: no diffusion channel formed at any time during ferrisiderophore uptake
    • Nader, M., Journet, L., Meksem, A., Guillon, L., Schalk, I.J., 2011. Mechanism of ferripyoverdine uptake by Pseudomonas aeruginosa outer membrane transporter FpvA: no diffusion channel formed at any time during ferrisiderophore uptake. Biochemistry 50, 2530-2540.
    • (2011) Biochemistry , vol.50 , pp. 2530-2540
    • Nader, M.1    Journet, L.2    Meksem, A.3    Guillon, L.4    Schalk, I.J.5
  • 116
    • 35448995327 scopus 로고    scopus 로고
    • Identification of residues of FpvA involved in the different steps of Pvd-Fe uptake in Pseudomonas aeruginosa
    • Nader, M., Dobbelaere, W., Vincent, M., Journet, L. et al., 2007. Identification of residues of FpvA involved in the different steps of Pvd-Fe uptake in Pseudomonas aeruginosa. Biochemistry 46, 11707-11717.
    • (2007) Biochemistry , vol.46 , pp. 11707-11717
    • Nader, M.1    Dobbelaere, W.2    Vincent, M.3    Journet, L.4
  • 117
    • 24044525255 scopus 로고    scopus 로고
    • Siderophore transport through Escherichia coli outer membrane receptor FhuA with disulfide-tethered cork and barrel domains
    • Eisenhauer, H.A., Shames, S., Pawelek, P.D., Coulton, J.W., 2005. Siderophore transport through Escherichia coli outer membrane receptor FhuA with disulfide-tethered cork and barrel domains. J. Biol. Chem. 280, 30574-30580.
    • (2005) J. Biol. Chem. , vol.280 , pp. 30574-30580
    • Eisenhauer, H.A.1    Shames, S.2    Pawelek, P.D.3    Coulton, J.W.4
  • 118
    • 0029906434 scopus 로고    scopus 로고
    • The Pseudomonas aeruginosa tonB gene encodes a novel TonB protein
    • Poole, K., Zhao, Q., Neshat, S., Heinrichs, D.E., Dean, C.R., 1996. The Pseudomonas aeruginosa tonB gene encodes a novel TonB protein. Microbiology 142, 1449-1458.
    • (1996) Microbiology , vol.142 , pp. 1449-1458
    • Poole, K.1    Zhao, Q.2    Neshat, S.3    Heinrichs, D.E.4    Dean, C.R.5
  • 119
    • 0033930584 scopus 로고    scopus 로고
    • Requirement of the Pseudomonas aeruginosa tonB gene for high-affinity iron acquisition and infection
    • Takase, H., Nitanai, H., Hoshino, K., Otani, T., 2000. Requirement of the Pseudomonas aeruginosa tonB gene for high-affinity iron acquisition and infection. Infect. Immun. 68, 4498-4504.
    • (2000) Infect. Immun. , vol.68 , pp. 4498-4504
    • Takase, H.1    Nitanai, H.2    Hoshino, K.3    Otani, T.4
  • 120
    • 0029155042 scopus 로고
    • Energy-coupled transport and signal transduction through the gram-negative outer membrane via TonB-ExbB-ExbD-dependent receptor proteins
    • Braun, V., 1995. Energy-coupled transport and signal transduction through the gram-negative outer membrane via TonB-ExbB-ExbD-dependent receptor proteins. FEMS Microbiol. Rev. 16, 295-307.
    • (1995) FEMS Microbiol. Rev. , vol.16 , pp. 295-307
    • Braun, V.1
  • 121
    • 33744791187 scopus 로고    scopus 로고
    • Structure of TonB in complex with FhuA, E. coli outer membrane receptor
    • Pawelek, P.D., Croteau, N., Ng-Thow-Hing, C., Khursigara, C.M. et al., 2006. Structure of TonB in complex with FhuA, E. coli outer membrane receptor. Science 312, 1399-1402.
    • (2006) Science , vol.312 , pp. 1399-1402
    • Pawelek, P.D.1    Croteau, N.2    Ng-Thow-Hing, C.3    Khursigara, C.M.4
  • 122
    • 33748657558 scopus 로고    scopus 로고
    • Interaction of TonB with the outer membrane receptor FpvA of Pseudomonas aeruginosa
    • Adams, H., Zeder-Lutz, G., Schalk, I., Pattus, F., Celia, H., 2006. Interaction of TonB with the outer membrane receptor FpvA of Pseudomonas aeruginosa. J. Bacteriol. 188, 5752-5761.
    • (2006) J. Bacteriol. , vol.188 , pp. 5752-5761
    • Adams, H.1    Zeder-Lutz, G.2    Schalk, I.3    Pattus, F.4    Celia, H.5
  • 123
    • 67651247345 scopus 로고    scopus 로고
    • Structure-function relationships in the bifunctional ferrisiderophore FpvA receptor from Pseudomonas aeruginosa
    • Schalk, I., Lamont, I., Cobessi, D., 2009. Structure-function relationships in the bifunctional ferrisiderophore FpvA receptor from Pseudomonas aeruginosa. BioMetals 22, 671-678.
    • (2009) BioMetals , vol.22 , pp. 671-678
    • Schalk, I.1    Lamont, I.2    Cobessi, D.3
  • 124
    • 69949105383 scopus 로고    scopus 로고
    • Role of TonB1 in pyoverdine-mediated signaling in Pseudomonas aeruginosa
    • Shirley, M., Lamont, I.L., 2009. Role of TonB1 in pyoverdine-mediated signaling in Pseudomonas aeruginosa. J. Bacteriol. 191, 5634-5640.
    • (2009) J. Bacteriol. , vol.191 , pp. 5634-5640
    • Shirley, M.1    Lamont, I.L.2
  • 125
    • 0037337264 scopus 로고    scopus 로고
    • Interactions between the outer membrane ferric citrate transporter FecA and TonB: studies of the FecA TonB box
    • Ogierman, M., Braun, V., 2003. Interactions between the outer membrane ferric citrate transporter FecA and TonB: studies of the FecA TonB box. J. Bacteriol. 185, 1870-1885.
    • (2003) J. Bacteriol. , vol.185 , pp. 1870-1885
    • Ogierman, M.1    Braun, V.2
  • 126
    • 79952796132 scopus 로고    scopus 로고
    • Legionella pneumophila LbtU acts as a novel, TonB-independent receptor for the legiobactin siderophore
    • Chatfield, C.H., Mulhern, B.J., Burnside, D.M., Cianciotto, N.P., 2011. Legionella pneumophila LbtU acts as a novel, TonB-independent receptor for the legiobactin siderophore. J. Bacteriol. 193, 1563-1575.
    • (2011) J. Bacteriol. , vol.193 , pp. 1563-1575
    • Chatfield, C.H.1    Mulhern, B.J.2    Burnside, D.M.3    Cianciotto, N.P.4
  • 127
    • 0348141912 scopus 로고    scopus 로고
    • Role of siderophore biosynthesis in virulence of Staphylococcus aureus: identification and characterization of genes involved in production of a siderophore
    • Dale, S.E., Doherty-Kirby, A., Lajoie, G., Heinrichs, D.E., 2004. Role of siderophore biosynthesis in virulence of Staphylococcus aureus: identification and characterization of genes involved in production of a siderophore. Infect. Immun. 72, 29-37.
    • (2004) Infect. Immun. , vol.72 , pp. 29-37
    • Dale, S.E.1    Doherty-Kirby, A.2    Lajoie, G.3    Heinrichs, D.E.4
  • 128
    • 33748500628 scopus 로고    scopus 로고
    • Ferribacillibactin uptake and hydrolysis in Bacillus subtilis
    • Miethke, M., Klotz, O., Linne, U., May, J.J. et al., 2006. Ferribacillibactin uptake and hydrolysis in Bacillus subtilis. Mol. Microbiol. 61, 1413-1427.
    • (2006) Mol. Microbiol. , vol.61 , pp. 1413-1427
    • Miethke, M.1    Klotz, O.2    Linne, U.3    May, J.J.4
  • 129
    • 33644872542 scopus 로고    scopus 로고
    • Requirement of Staphylococcus aureus ATP-binding cassette-ATPase FhuC for iron-restricted growth and evidence that It functions with more than one iron transporter
    • Speziali, C.D., Dale, S.E., Henderson, J.A., Vinés, E.D., Heinrichs, D.E., 2006. Requirement of Staphylococcus aureus ATP-binding cassette-ATPase FhuC for iron-restricted growth and evidence that It functions with more than one iron transporter. J. Bacteriol. 188, 2048-2055.
    • (2006) J. Bacteriol. , vol.188 , pp. 2048-2055
    • Speziali, C.D.1    Dale, S.E.2    Henderson, J.A.3    Vinés, E.D.4    Heinrichs, D.E.5
  • 130
    • 0036260950 scopus 로고    scopus 로고
    • Ferric hydroxamate binding protein FhuD from Escherichia coli: mutants in conserved and non-conserved regions
    • Clarke, T.E., Rohrbach, M.R., Tari, L.W., Vogel, H.J., Köster, W., 2002. Ferric hydroxamate binding protein FhuD from Escherichia coli: mutants in conserved and non-conserved regions. BioMetals 15, 121-131.
    • (2002) BioMetals , vol.15 , pp. 121-131
    • Clarke, T.E.1    Rohrbach, M.R.2    Tari, L.W.3    Vogel, H.J.4    Köster, W.5
  • 131
    • 0032763652 scopus 로고    scopus 로고
    • A multifunctional ATP-binding cassette transporter system from Vibrio cholerae transports vibriobactin and enterobactin
    • Wyckoff, E.E., Valle, A.M., Smith, S.L., Payne, S.M., 1999. A multifunctional ATP-binding cassette transporter system from Vibrio cholerae transports vibriobactin and enterobactin. J. Bacteriol. 181, 7588.
    • (1999) J. Bacteriol. , vol.181 , pp. 7588
    • Wyckoff, E.E.1    Valle, A.M.2    Smith, S.L.3    Payne, S.M.4
  • 132
    • 0032921490 scopus 로고    scopus 로고
    • YbtP and YbtQ: two ABC transporters required for iron uptake in Yersinia pestis
    • Fetherston, J.D., Bertolino, V.J., Perry, R.D., 1999. YbtP and YbtQ: two ABC transporters required for iron uptake in Yersinia pestis. Mol. Microbiol. 32, 289-299.
    • (1999) Mol. Microbiol. , vol.32 , pp. 289-299
    • Fetherston, J.D.1    Bertolino, V.J.2    Perry, R.D.3
  • 133
    • 0037341361 scopus 로고    scopus 로고
    • Molecular mechanisms of iron uptake in fungi
    • Kosman, D.J., 2003. Molecular mechanisms of iron uptake in fungi. Mol. Microbiol. 47, 1185-1197.
    • (2003) Mol. Microbiol. , vol.47 , pp. 1185-1197
    • Kosman, D.J.1
  • 134
    • 0026724913 scopus 로고
    • Overexpression and purification of ferric enterobactin esterase from Escherichia coli. Demonstration of enzymatic hydrolysis of enterobactin and its iron complex
    • Brickman, T.J., Mcintosh, M.A., 1992. Overexpression and purification of ferric enterobactin esterase from Escherichia coli. Demonstration of enzymatic hydrolysis of enterobactin and its iron complex. J. Biol. Chem. 267, 12350-12355.
    • (1992) J. Biol. Chem. , vol.267 , pp. 12350-12355
    • Brickman, T.J.1    Mcintosh, M.A.2
  • 135
    • 23744479843 scopus 로고    scopus 로고
    • In vitro characterization of salmochelin and enterobactin trilactone hydrolases IroD, IroE, and Fes
    • Lin, H., Fischbach, M.A., Liu, D.R., Walsh, C.T., 2005. In vitro characterization of salmochelin and enterobactin trilactone hydrolases IroD, IroE, and Fes. J. Am. Chem. Soc. 127, 11075-11084.
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 11075-11084
    • Lin, H.1    Fischbach, M.A.2    Liu, D.R.3    Walsh, C.T.4
  • 137
    • 0036887976 scopus 로고    scopus 로고
    • Chemistry for an essential biological process: the reduction of ferric iron
    • Pierre, J.L., Fontecave, M., Crichton, R.R., 2002. Chemistry for an essential biological process: the reduction of ferric iron. BioMetals 15, 341-346.
    • (2002) BioMetals , vol.15 , pp. 341-346
    • Pierre, J.L.1    Fontecave, M.2    Crichton, R.R.3
  • 138
    • 80055065227 scopus 로고    scopus 로고
    • New roles for bacterial siderophores in metal transport and tolerance
    • Schalk, I.J., Hannauer, M., Braud, A., 2011. New roles for bacterial siderophores in metal transport and tolerance. Environ. Microbiol. 13, 2844-2854.
    • (2011) Environ. Microbiol. , vol.13 , pp. 2844-2854
    • Schalk, I.J.1    Hannauer, M.2    Braud, A.3
  • 139
    • 0019447069 scopus 로고
    • Regulation of ferric iron transport in Escherichia coli K12: Isolation of a constitutive mutant
    • Hantke, K., 1981. Regulation of ferric iron transport in Escherichia coli K12: Isolation of a constitutive mutant. Mol. Gen. Genet. 182, 288-292.
    • (1981) Mol. Gen. Genet. , vol.182 , pp. 288-292
    • Hantke, K.1
  • 140
    • 28444438519 scopus 로고    scopus 로고
    • Iron and Fur regulation in Vibrio cholerae and the role of Fur in virulence
    • Mey, A.R., Wyckoff, E.E., Kanukurthy, V., Fisher, C.R., Payne, S.M., 2005. Iron and Fur regulation in Vibrio cholerae and the role of Fur in virulence. Infect. Immun. 73, 8167-8178.
    • (2005) Infect. Immun. , vol.73 , pp. 8167-8178
    • Mey, A.R.1    Wyckoff, E.E.2    Kanukurthy, V.3    Fisher, C.R.4    Payne, S.M.5
  • 141
    • 0344172832 scopus 로고    scopus 로고
    • Opening the iron box: transcriptional metalloregulation by the Fur protein
    • Escolar, L., Pérez-Martín, J., De Lorenzo, V., 1999. Opening the iron box: transcriptional metalloregulation by the Fur protein. J. Bacteriol. 181, 6223-6229.
    • (1999) J. Bacteriol. , vol.181 , pp. 6223-6229
    • Escolar, L.1    Pérez-Martín, J.2    De Lorenzo, V.3
  • 142
    • 0036302724 scopus 로고    scopus 로고
    • The gonococcal Fur regulon: identification of additional genes involved in major catabolic, recombination, and secretory pathways
    • Sebastian, S., Agarwal, S., Murphy, J.R., Genco, C.A., 2002. The gonococcal Fur regulon: identification of additional genes involved in major catabolic, recombination, and secretory pathways. J. Bacteriol. 184, 3965-3974.
    • (2002) J. Bacteriol. , vol.184 , pp. 3965-3974
    • Sebastian, S.1    Agarwal, S.2    Murphy, J.R.3    Genco, C.A.4
  • 143
    • 33748051446 scopus 로고    scopus 로고
    • Microbial evasion of the immune system: structural modifications of enterobactin impair siderocalin recognition 1
    • Abergel, R.J., Moore, E.G., Strong, R.K., Raymond, K.N., 2006. Microbial evasion of the immune system: structural modifications of enterobactin impair siderocalin recognition 1. J. Am. Chem. Soc. 128, 10998-10999.
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 10998-10999
    • Abergel, R.J.1    Moore, E.G.2    Strong, R.K.3    Raymond, K.N.4
  • 144
    • 79953033922 scopus 로고    scopus 로고
    • Secretion, but not overall synthesis, of catecholate siderophores contributes to virulence of extraintestinal pathogenic Escherichia coli
    • Caza, M., Lépine, F., Dozois, C.M., 2011. Secretion, but not overall synthesis, of catecholate siderophores contributes to virulence of extraintestinal pathogenic Escherichia coli. Mol. Microbiol. 80, 266-282.
    • (2011) Mol. Microbiol. , vol.80 , pp. 266-282
    • Caza, M.1    Lépine, F.2    Dozois, C.M.3
  • 145
    • 9444283787 scopus 로고    scopus 로고
    • Production by Escherichia coli isolates of siderophore and other virulence factors and their pathogenic role in a cutaneous infection model
    • Demir, M., Kaleli, I., 2004. Production by Escherichia coli isolates of siderophore and other virulence factors and their pathogenic role in a cutaneous infection model. Clin Microbiol. Infec. 10, 1011-1014.
    • (2004) Clin Microbiol. Infec. , vol.10 , pp. 1011-1014
    • Demir, M.1    Kaleli, I.2
  • 146
    • 33645049000 scopus 로고    scopus 로고
    • Iron acquisition systems for ferric hydroxamates, haemin and haemoglobin in Listeria monocytogenes
    • Jin, B., Newton, S.M.C., Shao, Y., Jiang, X. et al., 2006. Iron acquisition systems for ferric hydroxamates, haemin and haemoglobin in Listeria monocytogenes. Mol. Microbiol. 59, 1185-1198.
    • (2006) Mol. Microbiol. , vol.59 , pp. 1185-1198
    • Jin, B.1    Newton, S.M.C.2    Shao, Y.3    Jiang, X.4
  • 147
    • 79952485828 scopus 로고    scopus 로고
    • The TB structural genomics consortium: a decade of progress
    • Chim, N., Habel, J.E., Johnston, J.M., Krieger, I. et al., 2011. The TB structural genomics consortium: a decade of progress. Tuberculosis 91, 155-172.
    • (2011) Tuberculosis , vol.91 , pp. 155-172
    • Chim, N.1    Habel, J.E.2    Johnston, J.M.3    Krieger, I.4
  • 148
    • 38849128160 scopus 로고    scopus 로고
    • Biosynthesis and IroC-dependent export of the siderophore salmochelin are essential for virulence of Salmonella enterica serovar Typhimurium
    • Crouch, M-L.V., Castor, M., Karlinsey, J.E., Kalhorn, T., Fang, F.C., 2008. Biosynthesis and IroC-dependent export of the siderophore salmochelin are essential for virulence of Salmonella enterica serovar Typhimurium. Mol. Microbiol. 67, 971-983.
    • (2008) Mol. Microbiol. , vol.67 , pp. 971-983
    • Crouch, M.-L.1    Castor, M.2    Karlinsey, J.E.3    Kalhorn, T.4    Fang, F.C.5
  • 149
    • 33847713007 scopus 로고    scopus 로고
    • Yersiniabactin is a virulence factor for Klebsiella pneumoniae during pulmonary infection
    • Lawlor, M.S., O'connor, C., Miller, V.L., 2007. Yersiniabactin is a virulence factor for Klebsiella pneumoniae during pulmonary infection. Infect. Immun. 75, 1463.
    • (2007) Infect. Immun. , vol.75 , pp. 1463
    • Lawlor, M.S.1    O'connor, C.2    Miller, V.L.3
  • 150
    • 0030741108 scopus 로고    scopus 로고
    • Iron acquisition from transferrin and lactoferrin by Pseudomonas aeruginosa pyoverdine
    • Xiao, R., Kisaalita, W.S., 1997. Iron acquisition from transferrin and lactoferrin by Pseudomonas aeruginosa pyoverdine. Microbiology 143, 2509.
    • (1997) Microbiology , vol.143 , pp. 2509
    • Xiao, R.1    Kisaalita, W.S.2
  • 151
    • 0037198693 scopus 로고    scopus 로고
    • A component of innate immunity prevents bacterial biofilm development
    • Singh, P.K., Parsek, M.R., Greenberg, E.P., Welsh, M.J., 2002. A component of innate immunity prevents bacterial biofilm development. Nature 417, 552-555.
    • (2002) Nature , vol.417 , pp. 552-555
    • Singh, P.K.1    Parsek, M.R.2    Greenberg, E.P.3    Welsh, M.J.4
  • 152
    • 65449162362 scopus 로고    scopus 로고
    • Siderophore-mediated iron acquisition systems in Bacillus cereus: identification of receptors for anthrax virulence-associated petrobactin
    • Zawadzka, A.M., Abergel, R.J., Nichiporuk, R., Andersen, U.N., Raymond, K.N., 2009. Siderophore-mediated iron acquisition systems in Bacillus cereus: identification of receptors for anthrax virulence-associated petrobactin. Biochemistry 48, 3645-3657.
    • (2009) Biochemistry , vol.48 , pp. 3645-3657
    • Zawadzka, A.M.1    Abergel, R.J.2    Nichiporuk, R.3    Andersen, U.N.4    Raymond, K.N.5
  • 153
    • 0037076382 scopus 로고    scopus 로고
    • Siderophore-mediated signaling regulates virulence factor production in Pseudomonas aeruginosa
    • Lamont, I.L., Beare, P.A., Ochsner, U., Vasil, A.I., asil, M.L., 2002. Siderophore-mediated signaling regulates virulence factor production in Pseudomonas aeruginosa. Proc. Natl. Acad. Sci. 99, 7072-7077.
    • (2002) Proc. Natl. Acad. Sci. , vol.99 , pp. 7072-7077
    • Lamont, I.L.1    Beare, P.A.2    Ochsner, U.3    Vasil, A.I.4    Asil, M.L.5
  • 154
    • 67349110393 scopus 로고    scopus 로고
    • Siderophore production and biofilm formation as linked social traits
    • Harrison, F., Buckling, A., 2009. Siderophore production and biofilm formation as linked social traits. ISME J. 3, 632-634.
    • (2009) ISME J. , vol.3 , pp. 632-634
    • Harrison, F.1    Buckling, A.2
  • 155
    • 34748861878 scopus 로고    scopus 로고
    • The role of iron in Mycobacterium smegmatis biofilm formation: the exochelin siderophore is essential in limiting iron conditions for biofilm formation but not for planktonic growth
    • Ojha, A., Hatfull, G.F., 2007. The role of iron in Mycobacterium smegmatis biofilm formation: the exochelin siderophore is essential in limiting iron conditions for biofilm formation but not for planktonic growth. Mol. Microbiol. 66, 468-483.
    • (2007) Mol. Microbiol. , vol.66 , pp. 468-483
    • Ojha, A.1    Hatfull, G.F.2
  • 157
    • 0038641005 scopus 로고    scopus 로고
    • Phytoremediation: Synergistic use of plants and bacteria to clean up the environment
    • Glick, B.R., 2003. Phytoremediation: Synergistic use of plants and bacteria to clean up the environment. Biotechnol. Advances 21, 383-393.
    • (2003) Biotechnol. Advances , vol.21 , pp. 383-393
    • Glick, B.R.1
  • 158
    • 77952310876 scopus 로고    scopus 로고
    • Potential of siderophore-producing bacteria for improving heavy metal phytoextraction
    • Rajkumar, M., Ae, N., Prasad, M.N.V., Freitas, H., 2010. Potential of siderophore-producing bacteria for improving heavy metal phytoextraction. Trends Biotechnol 28, 142-149.
    • (2010) Trends Biotechnol , vol.28 , pp. 142-149
    • Rajkumar, M.1    Ae, N.2    Prasad, M.N.V.3    Freitas, H.4
  • 159
    • 56949102864 scopus 로고    scopus 로고
    • Metal-induced oxidative stress impacting plant growth in contaminated soil is alleviated by microbial siderophores
    • Dimkpa, C.O., Merten, D., Svatoš, A., Büchel, G., Kothe, E., 2009. Metal-induced oxidative stress impacting plant growth in contaminated soil is alleviated by microbial siderophores. Soil Biol. Biochem. 41, 154-162.
    • (2009) Soil Biol. Biochem. , vol.41 , pp. 154-162
    • Dimkpa, C.O.1    Merten, D.2    Svatoš, A.3    Büchel, G.4    Kothe, E.5
  • 160
    • 40849119743 scopus 로고    scopus 로고
    • Hydroxamate siderophores produced by Streptomyces acidiscabies E13 bind nickel and promote growth in cowpea (Vigna unguiculata) under nickel stress
    • Dimkpa, C.O., Svatoš, A., Merten, D., Büchel, G., Kothe, E., 2008. Hydroxamate siderophores produced by Streptomyces acidiscabies E13 bind nickel and promote growth in cowpea (Vigna unguiculata) under nickel stress. Can J Microbiol 54, 163-172.
    • (2008) Can J Microbiol , vol.54 , pp. 163-172
    • Dimkpa, C.O.1    Svatoš, A.2    Merten, D.3    Büchel, G.4    Kothe, E.5
  • 161
    • 70349947225 scopus 로고    scopus 로고
    • Siderophores mediate reduced and increased uptake of cadmium by Streptomyces tendae F4 and sunflower (Helianthus annuus), respectively
    • Dimkpa, C.O., Merten, D., Svatoš, A., Büchel, G., Kothe, E., 2009. Siderophores mediate reduced and increased uptake of cadmium by Streptomyces tendae F4 and sunflower (Helianthus annuus), respectively. J. Appl. Microbiol. 107, 1687-1696.
    • (2009) J. Appl. Microbiol. , vol.107 , pp. 1687-1696
    • Dimkpa, C.O.1    Merten, D.2    Svatoš, A.3    Büchel, G.4    Kothe, E.5
  • 162
    • 55649118894 scopus 로고    scopus 로고
    • Involvement of siderophores in the reduction of metal-induced inhibition of auxin synthesis in Streptomyces spp
    • Dimkpa, C.O., Svatoš, A., Dabrowska, P., Schmidt, A. et al., 2008. Involvement of siderophores in the reduction of metal-induced inhibition of auxin synthesis in Streptomyces spp. Chemosphere 74, 19-25.
    • (2008) Chemosphere , vol.74 , pp. 19-25
    • Dimkpa, C.O.1    Svatoš, A.2    Dabrowska, P.3    Schmidt, A.4
  • 163
    • 56549091178 scopus 로고    scopus 로고
    • Enhanced phytoextraction of an agricultural cr- and pb-contaminated soil by bioaugmentation with siderophore-producing bacteria
    • Braud, A., Jézéquel, K., Bazot, S., Lebeau, T., 2009. Enhanced phytoextraction of an agricultural cr- and pb-contaminated soil by bioaugmentation with siderophore-producing bacteria. Chemosphere 74, 280-286.
    • (2009) Chemosphere , vol.74 , pp. 280-286
    • Braud, A.1    Jézéquel, K.2    Bazot, S.3    Lebeau, T.4
  • 165
    • 77951504504 scopus 로고
    • Pseudomonas siderophores: A mechanism explaining disease-suppressive soils
    • Kloepper, J., Leong, J., Teintze, M., Schroth, M., 1980. Pseudomonas siderophores: A mechanism explaining disease-suppressive soils. Curr Microbiol 4, 317-320.
    • (1980) Curr Microbiol , vol.4 , pp. 317-320
    • Kloepper, J.1    Leong, J.2    Teintze, M.3    Schroth, M.4
  • 166
    • 15944409255 scopus 로고    scopus 로고
    • Biological control of soil-borne pathogens by fluorescent pseudomonads
    • Haas, D., Defago, G., 2005. Biological control of soil-borne pathogens by fluorescent pseudomonads. Nat Rev Micro 3, 307-319.
    • (2005) Nat Rev Micro , vol.3 , pp. 307-319
    • Haas, D.1    Defago, G.2
  • 167
    • 64849116031 scopus 로고    scopus 로고
    • Pseudomonas fluorescens and closely-related fluorescent pseudomonads as biocontrol agents of soil-borne phytopathogens
    • Couillerot, O., Prigent-Combaret, C., Caballero-Mellado, J., Moënne-Loccoz, Y., 2009. Pseudomonas fluorescens and closely-related fluorescent pseudomonads as biocontrol agents of soil-borne phytopathogens. Lett. Appl. Microbiol. 48, 505-512.
    • (2009) Lett. Appl. Microbiol. , vol.48 , pp. 505-512
    • Couillerot, O.1    Prigent-Combaret, C.2    Caballero-Mellado, J.3    Moënne-Loccoz, Y.4
  • 168
    • 33846477184 scopus 로고    scopus 로고
    • Pseudomonas biocontrol agents of soilborne pathogens: Looking back over 30 years
    • Weller, D.M., 2007. Pseudomonas biocontrol agents of soilborne pathogens: Looking back over 30 years. Phytopathology 97, 250-256.
    • (2007) Phytopathology , vol.97 , pp. 250-256
    • Weller, D.M.1
  • 169
    • 80055093178 scopus 로고    scopus 로고
    • Disease control and plant growth promotion of green gram by siderophore producing Pseudomonas sp
    • Sahu, G., Sindhu, S., 2011. Disease control and plant growth promotion of green gram by siderophore producing Pseudomonas sp. Res. J. Microbiol. 6, 735-749.
    • (2011) Res. J. Microbiol. , vol.6 , pp. 735-749
    • Sahu, G.1    Sindhu, S.2
  • 170
    • 77951572955 scopus 로고    scopus 로고
    • Impact of siderophore production by Pseudomonas syringae pv. syringae 22d/93 on epiphytic fitness and biocontrol activity against Pseudomonas syringae pv. glycinea 1a/96
    • Wensing, A., Braun, S.D., Büttner, P., Expert, D. et al., 2010. Impact of siderophore production by Pseudomonas syringae pv. syringae 22d/93 on epiphytic fitness and biocontrol activity against Pseudomonas syringae pv. glycinea 1a/96. Appl. Environ. Microbiol. 76, 2704-2711.
    • (2010) Appl. Environ. Microbiol. , vol.76 , pp. 2704-2711
    • Wensing, A.1    Braun, S.D.2    Büttner, P.3    Expert, D.4
  • 171
    • 3042925626 scopus 로고
    • Spectrophotometric determination of vanadium(v) with Desferrioxamine B
    • Luterotti, S., Grdinic, V., 1986. Spectrophotometric determination of vanadium(v) with Desferrioxamine B. Analyst 111, 1163-1165.
    • (1986) Analyst , vol.111 , pp. 1163-1165
    • Luterotti, S.1    Grdinic, V.2
  • 172
    • 0001140298 scopus 로고    scopus 로고
    • Stability constants for complexes of the siderophore desferrioxamine b with selected heavy metal cations
    • Hernlem, B.J., Vane, L.M., Sayles, G.D., 1996. Stability constants for complexes of the siderophore desferrioxamine b with selected heavy metal cations. Inorg. Chim. Acta 244, 179-184.
    • (1996) Inorg. Chim. Acta , vol.244 , pp. 179-184
    • Hernlem, B.J.1    Vane, L.M.2    Sayles, G.D.3
  • 173
    • 0034678886 scopus 로고    scopus 로고
    • Structural characterization of a plutonium(iv) siderophore complex: Single-crystal structure of Pu-Desferrioxamine E
    • Neu, M.P., Matonic, J.H., Ruggiero, C.E., Scott, B.L., 2000. Structural characterization of a plutonium(iv) siderophore complex: Single-crystal structure of Pu-Desferrioxamine E. Angew. Chem. Int. Edit. 39, 1442-1444.
    • (2000) Angew. Chem. Int. Edit. , vol.39 , pp. 1442-1444
    • Neu, M.P.1    Matonic, J.H.2    Ruggiero, C.E.3    Scott, B.L.4
  • 174
    • 65349127542 scopus 로고    scopus 로고
    • New insights into the metal specificity of the Pseudomonas aeruginosa pyoverdine-iron uptake pathway
    • Braud, A., Hoegy, F., Jezequel, K., Lebeau, T., Schalk, I.J., 2009. New insights into the metal specificity of the Pseudomonas aeruginosa pyoverdine-iron uptake pathway. Environ. Microbiol. 11, 1079-1091.
    • (2009) Environ. Microbiol. , vol.11 , pp. 1079-1091
    • Braud, A.1    Hoegy, F.2    Jezequel, K.3    Lebeau, T.4    Schalk, I.J.5
  • 175
    • 78649732156 scopus 로고    scopus 로고
    • Presence of the siderophores pyoverdine and pyochelin in the extracellular medium reduces toxic metal accumulation in pseudomonas aeruginosa and increases bacterial metal tolerance
    • Braud, A., Geoffroy, V., Hoegy, F., Mislin, G.L.A., Schalk, I.J., 2010. Presence of the siderophores pyoverdine and pyochelin in the extracellular medium reduces toxic metal accumulation in pseudomonas aeruginosa and increases bacterial metal tolerance. Environ. Microbiol. R. 2, 419-425.
    • (2010) Environ. Microbiol. R. , vol.2 , pp. 419-425
    • Braud, A.1    Geoffroy, V.2    Hoegy, F.3    Mislin, G.L.A.4    Schalk, I.J.5
  • 176
    • 0031784427 scopus 로고    scopus 로고
    • The stability of the molybdenum-azotochelin complex and its effect on siderophore production in Azotobacter vinelandii
    • Duhme, A.K., Hider, R., Naldrett, M., Pau, R., 1998. The stability of the molybdenum-azotochelin complex and its effect on siderophore production in Azotobacter vinelandii. J. Biol. Inorg. Chem. 3, 520-526.
    • (1998) J. Biol. Inorg. Chem. , vol.3 , pp. 520-526
    • Duhme, A.K.1    Hider, R.2    Naldrett, M.3    Pau, R.4
  • 177
    • 0029805914 scopus 로고    scopus 로고
    • Siderophore-mediated aluminum uptake by Bacillus megaterium ATCC 19213
    • Hu, X., Boyer, G.L., 1996. Siderophore-mediated aluminum uptake by Bacillus megaterium ATCC 19213. Appl. Environ. Microbiol. 62, 4044-4048.
    • (1996) Appl. Environ. Microbiol. , vol.62 , pp. 4044-4048
    • Hu, X.1    Boyer, G.L.2
  • 178
    • 26944468295 scopus 로고    scopus 로고
    • Pchr-box recognition by the Arac-type regulator pchr of Pseudomonas aeruginosa requires the siderophore pyochelin as an effector
    • Michel, L., González, N., Jagdeep, S., Nguyen-Ngoc, T., Reimmann, C., 2005. Pchr-box recognition by the Arac-type regulator pchr of Pseudomonas aeruginosa requires the siderophore pyochelin as an effector. Mol. Microbiol. 58, 495-509.
    • (2005) Mol. Microbiol. , vol.58 , pp. 495-509
    • Michel, L.1    González, N.2    Jagdeep, S.3    Nguyen-Ngoc, T.4    Reimmann, C.5
  • 179
    • 0035887796 scopus 로고    scopus 로고
    • Biofilm formation: A clinically relevant microbiological process
    • Donlan, R.M., 2001. Biofilm formation: A clinically relevant microbiological process. Clin. Infect. Dis. 33, 1387-1392.
    • (2001) Clin. Infect. Dis. , vol.33 , pp. 1387-1392
    • Donlan, R.M.1
  • 180
    • 39649107354 scopus 로고    scopus 로고
    • Bacterial and fungal biofilm infections
    • Lynch, A.S., Robertson, G.T., 2008. Bacterial and fungal biofilm infections. Annu. Rev. Med. 59, 415-428.
    • (2008) Annu. Rev. Med. , vol.59 , pp. 415-428
    • Lynch, A.S.1    Robertson, G.T.2
  • 181
    • 0142031760 scopus 로고    scopus 로고
    • Biofilms: A clinical perspective
    • Bell, M., 2001. Biofilms: A clinical perspective. Curr. Infect. Dis. R. 3, 483-486.
    • (2001) Curr. Infect. Dis. R. , vol.3 , pp. 483-486
    • Bell, M.1
  • 182
    • 0033591467 scopus 로고    scopus 로고
    • Bacterial biofilms: A common cause of persistent infections
    • Costerton, J.W., Stewart, P.S., Greenberg, E.P., 1999. Bacterial biofilms: A common cause of persistent infections. Science 284, 1318-1322.
    • (1999) Science , vol.284 , pp. 1318-1322
    • Costerton, J.W.1    Stewart, P.S.2    Greenberg, E.P.3
  • 184
    • 0034057759 scopus 로고    scopus 로고
    • Biofilm resistance to antimicrobial agents
    • Xu, K.D., McFeters, G.A., Stewart, P.S., 2000. Biofilm resistance to antimicrobial agents. Microbiology 146, 547.
    • (2000) Microbiology , vol.146 , pp. 547
    • Xu, K.D.1    McFeters, G.A.2    Stewart, P.S.3
  • 185
    • 0035859467 scopus 로고    scopus 로고
    • Antibiotic resistance of bacteria in biofilms
    • Stewart, P.S., William Costerton, J., 2001. Antibiotic resistance of bacteria in biofilms. The Lancet 358, 135-138.
    • (2001) The Lancet , vol.358 , pp. 135-138
    • Stewart, P.S.1    William Costerton, J.2
  • 186
    • 34748861878 scopus 로고    scopus 로고
    • The role of iron in Mycobacterium smegmatis biofilm formation: The exochelin siderophore is essential in limiting iron conditions for biofilm formation but not for planktonic growth
    • Ojha, A., Hatfull, G.F., 2007. The role of iron in Mycobacterium smegmatis biofilm formation: The exochelin siderophore is essential in limiting iron conditions for biofilm formation but not for planktonic growth. Mol. Microbiol. 66, 468-483.
    • (2007) Mol. Microbiol. , vol.66 , pp. 468-483
    • Ojha, A.1    Hatfull, G.F.2
  • 187
    • 59449105814 scopus 로고    scopus 로고
    • Utilization of microbial iron assimilation processes for the development of new antibiotics and inspiration for the design of new anticancer agents
    • Miller, M., Zhu, H., Xu, Y., Wu, C. et al., 2009. Utilization of microbial iron assimilation processes for the development of new antibiotics and inspiration for the design of new anticancer agents. BioMetals 22, 61-75.
    • (2009) BioMetals , vol.22 , pp. 61-75
    • Miller, M.1    Zhu, H.2    Xu, Y.3    Wu, C.4
  • 188
    • 67651247638 scopus 로고    scopus 로고
    • Siderophores as drug delivery agents: application of the "Trojan Horse" strategy
    • Möllmann, U., Heinisch, L., Bauernfeind, A., Köhler, T., Ankel-Fuchs, D., 2009. Siderophores as drug delivery agents: application of the "Trojan Horse" strategy. BioMetals 22, 615-624.
    • (2009) BioMetals , vol.22 , pp. 615-624
    • Möllmann, U.1    Heinisch, L.2    Bauernfeind, A.3    Köhler, T.4    Ankel-Fuchs, D.5
  • 190
    • 78650656571 scopus 로고    scopus 로고
    • Structural basis for effectiveness of siderophore-conjugated monocarbams against clinically relevant strains of Pseudomonas aeruginosa
    • Han, S., Zaniewski, R.P., Marr, E.S., Lacey, B.M. et al., 2010. Structural basis for effectiveness of siderophore-conjugated monocarbams against clinically relevant strains of Pseudomonas aeruginosa. Proc. Natl. Acad. Sci. 107, 22002-22007.
    • (2010) Proc. Natl. Acad. Sci. , vol.107 , pp. 22002-22007
    • Han, S.1    Zaniewski, R.P.2    Marr, E.S.3    Lacey, B.M.4
  • 191
    • 0037236867 scopus 로고    scopus 로고
    • Synthesis and biological activity of tris-and tetrakiscatecholate siderophores based on poly-aza alkanoic acids or alkylbenzoic acids and their conjugates with beta-lactam antibiotics
    • Heinisch, L., Wittmann, S., Stoiber, T., Scherlitz-Hofmann, I. et al., 2003. Synthesis and biological activity of tris-and tetrakiscatecholate siderophores based on poly-aza alkanoic acids or alkylbenzoic acids and their conjugates with beta-lactam antibiotics. Arzneimittel-Forschung. 53, 188.
    • (2003) Arzneimittel-Forschung. , vol.53 , pp. 188
    • Heinisch, L.1    Wittmann, S.2    Stoiber, T.3    Scherlitz-Hofmann, I.4
  • 192
    • 79951816261 scopus 로고    scopus 로고
    • Design, synthesis, and study of a mycobactin-artemisinin conjugate that has selective and potent activity against tuberculosis and malaria
    • Miller, M.J., Walz, A.J., Zhu, H., Wu, C. et al., 2011. Design, synthesis, and study of a mycobactin-artemisinin conjugate that has selective and potent activity against tuberculosis and malaria. J. Am. Chem. Soc. 133, 2076-2079.
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 2076-2079
    • Miller, M.J.1    Walz, A.J.2    Zhu, H.3    Wu, C.4
  • 194
    • 34147096980 scopus 로고    scopus 로고
    • The transition metal gallium disrupts Pseudomonas aeruginosa iron metabolism and has antimicrobial and antibiofilm activity
    • Kaneko, Y., Thoendel, M., Olakanmi, O., Britigan, B.E., Singh, P.K., 2007. The transition metal gallium disrupts Pseudomonas aeruginosa iron metabolism and has antimicrobial and antibiofilm activity. J. Clin. Invest. 117, 877.
    • (2007) J. Clin. Invest. , vol.117 , pp. 877
    • Kaneko, Y.1    Thoendel, M.2    Olakanmi, O.3    Britigan, B.E.4    Singh, P.K.5
  • 195
    • 33644933286 scopus 로고    scopus 로고
    • Chelator-induced dispersal and killing of Pseudomonas aeruginosa cells in a biofilm
    • Banin, E., Brady, K.M., Greenberg, E.P., 2006. Chelator-induced dispersal and killing of Pseudomonas aeruginosa cells in a biofilm. Appl. Environ. Microbiol. 72, 2064-2069.
    • (2006) Appl. Environ. Microbiol. , vol.72 , pp. 2064-2069
    • Banin, E.1    Brady, K.M.2    Greenberg, E.P.3
  • 197
    • 47249121254 scopus 로고    scopus 로고
    • Chelated iron sources are inhibitors of Pseudomonas aeruginosa biofilms and distribute efficiently in an in vitro model of drug delivery to the human lung
    • Musk, D.J., Hergenrother, P.J., 2008. Chelated iron sources are inhibitors of Pseudomonas aeruginosa biofilms and distribute efficiently in an in vitro model of drug delivery to the human lung. J. Appl. Microbiol. 105, 380-388.
    • (2008) J. Appl. Microbiol. , vol.105 , pp. 380-388
    • Musk, D.J.1    Hergenrother, P.J.2
  • 198
    • 66449094685 scopus 로고    scopus 로고
    • Iron-binding compounds impair Pseudomonas aeruginosa biofilm formation, especially under anaerobic conditions
    • O'may, C.Y., Sanderson, K., Roddam, L.F., Kirov, S.M., Reid, D.W., 2009. Iron-binding compounds impair Pseudomonas aeruginosa biofilm formation, especially under anaerobic conditions. J. Med. Microbiol. 58, 765-773.
    • (2009) J. Med. Microbiol. , vol.58 , pp. 765-773
    • O'may, C.Y.1    Sanderson, K.2    Roddam, L.F.3    Kirov, S.M.4    Reid, D.W.5
  • 199
    • 69449107153 scopus 로고    scopus 로고
    • Tobramycin and FDA-approved iron chelators eliminate P. aeruginosa biofilms on cystic fibrosis cells
    • Moreau-Marquis, S., O'toole, G.A., Stanton, B.A., 2009. Tobramycin and FDA-approved iron chelators eliminate P. aeruginosa biofilms on cystic fibrosis cells. Am. J. Respir. Cell Mol. Biol. 41, 305-313.
    • (2009) Am. J. Respir. Cell Mol. Biol. , vol.41 , pp. 305-313
    • Moreau-Marquis, S.1    O'toole, G.A.2    Stanton, B.A.3
  • 200
    • 0016591187 scopus 로고
    • The effect of p-aminosalicyclic acid on iron transport and assimilation in mycobacteria
    • Brown, K.A., Ratledge, C., 1975. The effect of p-aminosalicyclic acid on iron transport and assimilation in mycobacteria. Biochim. Biophys. Acta. 385, 207-220.
    • (1975) Biochim. Biophys. Acta. , vol.385 , pp. 207-220
    • Brown, K.A.1    Ratledge, C.2
  • 201
    • 33344469904 scopus 로고    scopus 로고
    • Small-molecule inhibition of siderophore biosynthesis in Mycobacterium tuberculosis and Yersinia pestis
    • Ferreras, J.A., Ryu, J-S., Di Lello, F., Tan, D.S., Quadri, L.E.N., 2005. Small-molecule inhibition of siderophore biosynthesis in Mycobacterium tuberculosis and Yersinia pestis. Nat. Chem. Biol. 1, 29-32.
    • (2005) Nat. Chem. Biol. , vol.1 , pp. 29-32
    • Ferreras, J.A.1    Ryu, J.-S.2    Di Lello, F.3    Tan, D.S.4    Quadri, L.E.N.5
  • 202
    • 78049279393 scopus 로고    scopus 로고
    • Biochemical and structural characterization of bisubstrate inhibitors of BasE, the self-standing nonribosomal peptide synthetase adenylate-forming enzyme ofaAcinetobactin synthesis
    • Drake, E.J., Duckworth, B.P., Neres, J.O., Aldrich, C.C., Gulick, A.M., 2010. Biochemical and structural characterization of bisubstrate inhibitors of BasE, the self-standing nonribosomal peptide synthetase adenylate-forming enzyme ofaAcinetobactin synthesis. Biochemistry 49, 9292-9305.
    • (2010) Biochemistry , vol.49 , pp. 9292-9305
    • Drake, E.J.1    Duckworth, B.P.2    Neres, J.O.3    Aldrich, C.C.4    Gulick, A.M.5
  • 203
    • 0035352919 scopus 로고    scopus 로고
    • Siderotyping a powerful tool for the characterization of pyoverdines
    • Fuchs, R., Schafer, M., Geoffroy, V., Meyer, J.M., 2001. Siderotyping a powerful tool for the characterization of pyoverdines. Curr. Top. Med. Chem. 1, 31-57.
    • (2001) Curr. Top. Med. Chem. , vol.1 , pp. 31-57
    • Fuchs, R.1    Schafer, M.2    Geoffroy, V.3    Meyer, J.M.4
  • 204
    • 36549004063 scopus 로고    scopus 로고
    • Taxonomic heterogeneity, as shown by siderotyping, of strains primarily identified as Pseudomonas putida
    • Meyer, J-M., Gruffaz, C., Tulkki, T., Izard, D., 2007. Taxonomic heterogeneity, as shown by siderotyping, of strains primarily identified as Pseudomonas putida. Int. J. Syst. Evol. Microbiol. 57, 2543-2556.
    • (2007) Int. J. Syst. Evol. Microbiol. , vol.57 , pp. 2543-2556
    • Meyer, J.-M.1    Gruffaz, C.2    Tulkki, T.3    Izard, D.4
  • 205
    • 55849135185 scopus 로고    scopus 로고
    • Phylogenetic analysis and siderotyping as useful tools in the taxonomy of Pseudomonas stutzeri: description of a novel genomovar
    • Mulet, M., Gomila, M., Gruffaz, C., Meyer, J-M. et al., 2008. Phylogenetic analysis and siderotyping as useful tools in the taxonomy of Pseudomonas stutzeri: description of a novel genomovar. Int. J. Syst. Evol. Microbiol. 58, 2309-2315.
    • (2008) Int. J. Syst. Evol. Microbiol. , vol.58 , pp. 2309-2315
    • Mulet, M.1    Gomila, M.2    Gruffaz, C.3    Meyer, J.-M.4
  • 206
    • 42549136915 scopus 로고    scopus 로고
    • Siderotyping of fluorescent-pseudomonas: molecular mass determination by mass spectrometry as a powerful pyoverdine siderotyping method
    • Meyer, J-M., Gruffaz, C., Raharinosy, V., Bezverbnaya, I. et al., 2008. Siderotyping of fluorescent-pseudomonas: molecular mass determination by mass spectrometry as a powerful pyoverdine siderotyping method. BioMetals 21, 259-271.
    • (2008) BioMetals , vol.21 , pp. 259-271
    • Meyer, J.-M.1    Gruffaz, C.2    Raharinosy, V.3    Bezverbnaya, I.4
  • 207
    • 84876446538 scopus 로고    scopus 로고
    • Pyoverdine siderophores as taxonomic markers
    • Ramos, J.L., Filloux, A., eds., Springer, Netherlands.
    • Meyer, J.M., 2010. Pyoverdine siderophores as taxonomic markers. In: Ramos, J.L., Filloux, A., (eds.), Pseudomonas. Springer, Netherlands.
    • (2010) Pseudomonas
    • Meyer, J.M.1
  • 208
    • 77956468213 scopus 로고    scopus 로고
    • Development of a real-time TaqMan assay to detect mendocina sublineage Pseudomonas species in contaminated metal working fluids
    • Saha, R., Donofrio, R.S., Bagley, S.T., 2010. Development of a real-time TaqMan assay to detect mendocina sublineage Pseudomonas species in contaminated metal working fluids. J. Ind. Microbiol. Biotechnol. 37, 843-848.
    • (2010) J. Ind. Microbiol. Biotechnol. , vol.37 , pp. 843-848
    • Saha, R.1    Donofrio, R.S.2    Bagley, S.T.3
  • 209
    • 77949545789 scopus 로고    scopus 로고
    • Siderophores from neighboring organisms promote the growth of uncultured bacteria
    • D'onofrio, A., Crawford, J.M., Stewart, E.J., Witt, K. et al., 2010. Siderophores from neighboring organisms promote the growth of uncultured bacteria. Chemistry & Biology 17, 254-264.
    • (2010) Chemistry & Biology , vol.17 , pp. 254-264
    • D'onofrio, A.1    Crawford, J.M.2    Stewart, E.J.3    Witt, K.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.