메뉴 건너뛰기




Volumn 2, Issue 3, 2006, Pages 132-138

How pathogenic bacteria evade mammalian sabotage in the battle for iron

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; ENTEROCHELIN; IRON; SCAVENGER; SIDEROPHORE; DRUG DERIVATIVE; GLUCOSIDE; SERINE;

EID: 33646593180     PISSN: 15524450     EISSN: 15524469     Source Type: Journal    
DOI: 10.1038/nchembio771     Document Type: Review
Times cited : (250)

References (79)
  • 1
    • 0034595617 scopus 로고    scopus 로고
    • Lack of a role for iron in the Lyme disease pathogen
    • Posey, J.E. & Gherardini, F.C. Lack of a role for iron in the Lyme disease pathogen. Science 288, 1651-1653 (2000).
    • (2000) Science , vol.288 , pp. 1651-1653
    • Posey, J.E.1    Gherardini, F.C.2
  • 2
    • 0030667658 scopus 로고    scopus 로고
    • The Lactobacillus anomaly: Total iron abstinence
    • Weinberg, E.D. The Lactobacillus anomaly: total iron abstinence. Perspect. Biol. Med. 40, 578-583 (1997).
    • (1997) Perspect. Biol. Med. , vol.40 , pp. 578-583
    • Weinberg, E.D.1
  • 3
    • 0037389797 scopus 로고    scopus 로고
    • Enterobactin: An archetype for microbial iron transport
    • Raymond, K.N., Dertz, E.A. & Kim, S.S. Enterobactin: an archetype for microbial iron transport. Proc. Natl Acad. Sci. USA 100, 3584-3588 (2003).
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 3584-3588
    • Raymond, K.N.1    Dertz, E.A.2    Kim, S.S.3
  • 5
    • 0036280341 scopus 로고    scopus 로고
    • Genetics and assembly line enzymology of siderophore biosynthesis in bacteria
    • Crosa, J.H. & Walsh, C.T. Genetics and assembly line enzymology of siderophore biosynthesis in bacteria. Microbiol. Mol. Biol. Rev. 66, 223-249 (2002).
    • (2002) Microbiol. Mol. Biol. Rev. , vol.66 , pp. 223-249
    • Crosa, J.H.1    Walsh, C.T.2
  • 6
    • 0032562142 scopus 로고    scopus 로고
    • Reconstitution and characterization of the Escherichia coli enterobactin synthetase from EntB, EntE, and EntF
    • Gehring, A.M., Mori, I. & Walsh, C.T. Reconstitution and characterization of the Escherichia coli enterobactin synthetase from EntB, EntE, and EntF. Biochemistry 37, 2648-2659 (1998).
    • (1998) Biochemistry , vol.37 , pp. 2648-2659
    • Gehring, A.M.1    Mori, I.2    Walsh, C.T.3
  • 7
    • 0001293075 scopus 로고
    • Molecular studies on enzymes in chorismate metabolism and the enterobactin biosynthetic pathway
    • Walsh, C., Liu, J., Rusnak, F. & Sakaitani, M. Molecular studies on enzymes in chorismate metabolism and the enterobactin biosynthetic pathway. Chem. Rev. 90, 1105-1129 (1990).
    • (1990) Chem. Rev. , vol.90 , pp. 1105-1129
    • Walsh, C.1    Liu, J.2    Rusnak, F.3    Sakaitani, M.4
  • 8
    • 0030294470 scopus 로고    scopus 로고
    • A new enzyme superfamily - The phosphopantetheinyl transferases
    • Lambalot, R.H. et al. A new enzyme superfamily - the phosphopantetheinyl transferases. Chem. Biol. 3, 923-936 (1996).
    • (1996) Chem. Biol. , vol.3 , pp. 923-936
    • Lambalot, R.H.1
  • 9
    • 0036015639 scopus 로고    scopus 로고
    • Export of the siderophore enterobactin in Escherichia coli: Involvement of a 43 kDa membrane exporter
    • Furrer, J.L., Sanders, D.N., Hook-Barnard, I.G. & McIntosh, M.A. Export of the siderophore enterobactin in Escherichia coli: involvement of a 43 kDa membrane exporter. Mol. Microbiol. 44, 1225-1234 (2002).
    • (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
  • 10
    • 25144462979 scopus 로고    scopus 로고
    • TolC is involved in enterobactin efflux across the outer membrane of Escherichia coli
    • Bleuel, C. et al. TolC is involved in enterobactin efflux across the outer membrane of Escherichia coli. J. Bacteriol. 187, 6701-6707 (2005).
    • (2005) J. Bacteriol. , vol.187 , pp. 6701-6707
    • Bleuel, C.1
  • 13
    • 0032900438 scopus 로고    scopus 로고
    • Crystal structure of the outer membrane active transporter FepA from Escherichia coli
    • Buchanan, S.K. et al. Crystal structure of the outer membrane active transporter FepA from Escherichia coli. Nat. Struct. Biol. 6, 56-63 (1999).
    • (1999) Nat. Struct. Biol. , vol.6 , pp. 56-63
    • Buchanan, S.K.1
  • 14
    • 0037317173 scopus 로고    scopus 로고
    • Acquisition of siderophores in gram-negative bacteria
    • Faraldo-Gomez, J.D. & Sansom, M.S. Acquisition of siderophores in gram-negative bacteria. Nat. Rev. Mol. Cell Biol. 4, 105-116 (2003).
    • (2003) Nat. Rev. Mol. Cell Biol. , vol.4 , pp. 105-116
    • Faraldo-Gomez, J.D.1    Sansom, M.S.2
  • 15
    • 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. In vitro characterization of salmochelin and enterobactin trilactone hydrolases IroD, IroE, and Fes. J. Am. Chem. Soc. 127, 11075-11084 (2005).
    • (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
  • 16
    • 0035069457 scopus 로고    scopus 로고
    • Iron and metal regulation in bacteria
    • Hantke, K. Iron and metal regulation in bacteria. Curr. Opin. Microbiol. 4, 172-177 (2001).
    • (2001) Curr. Opin. Microbiol. , vol.4 , pp. 172-177
    • Hantke, K.1
  • 17
    • 0001569222 scopus 로고
    • Coordination chemistry of microbial iron transport compounds. 19. Stability constants and electrochemical behavior of ferric enterobactin and model complexes
    • Harris, W.R. et al. Coordination chemistry of microbial iron transport compounds. 19. Stability constants and electrochemical behavior of ferric enterobactin and model complexes. J. Am. Chem. Soc. 101, 6097-6104 (1979).
    • (1979) J. Am. Chem. Soc. , vol.101 , pp. 6097-6104
    • Harris, W.R.1
  • 18
    • 21044449406 scopus 로고    scopus 로고
    • A widely distributed bacterial pathway for siderophore biosynthesis independent of nonribosomal peptide synthetases
    • Challis, G.L. A widely distributed bacterial pathway for siderophore biosynthesis independent of nonribosomal peptide synthetases. ChemBioChem 6, 601-611 (2005).
    • (2005) ChemBioChem , vol.6 , pp. 601-611
    • Challis, G.L.1
  • 19
    • 0001569223 scopus 로고
    • Coordination chemistry of microbial iron transport compounds. 16. Isolation, characterization, and formation constants of ferric aerobactin
    • Harris, W.R., Carrano, C.J. & Raymond, K.N. Coordination chemistry of microbial iron transport compounds. 16. Isolation, characterization, and formation constants of ferric aerobactin. J. Am. Chem. Soc. 110, 2722-2727 (1979).
    • (1979) J. Am. Chem. Soc. , vol.110 , pp. 2722-2727
    • Harris, W.R.1    Carrano, C.J.2    Raymond, K.N.3
  • 20
    • 0025886812 scopus 로고
    • Relative availability of transferrin-bound iron and cell-derived iron to aerobactin-producing and enterochelin-producing strains of Escherichia coli and to other microorganisms
    • Brock, J.H., Williams, P.H., Liceaga, J. & Wooldridge, K.G. Relative availability of transferrin-bound iron and cell-derived iron to aerobactin-producing and enterochelin-producing strains of Escherichia coli and to other microorganisms. Infect. Immun. 59, 3185-3190 (1991).
    • (1991) Infect. Immun. , vol.59 , pp. 3185-3190
    • Brock, J.H.1    Williams, P.H.2    Liceaga, J.3    Wooldridge, K.G.4
  • 21
    • 0023851580 scopus 로고
    • Differences in excretion and efficiency of the aerobactin and enterochelin siderophores in a bovine pathogenic strain of Escherichia coli
    • Der Vartanian, M. Differences in excretion and efficiency of the aerobactin and enterochelin siderophores in a bovine pathogenic strain of Escherichia coli. Infect. Immun. 56, 413-418 (1988).
    • (1988) Infect. Immun. , vol.56 , pp. 413-418
    • Der Vartanian, M.1
  • 22
    • 0020448368 scopus 로고
    • Aerobactin-mediated utilization of transferrin iron
    • Konopka, K., Bindereif, A. & Neilands, J.B. Aerobactin-mediated utilization of transferrin iron. Biochemistry 21, 6503-6508 (1982).
    • (1982) Biochemistry , vol.21 , pp. 6503-6508
    • Konopka, K.1    Bindereif, A.2    Neilands, J.B.3
  • 23
    • 0022576611 scopus 로고
    • Iron, siderophores, and the pursuit of virulence: Independence of the aerobactin and enterochelin iron uptake systems in Escherichia coli
    • Williams, P.H. & Carbonetti, N.H. Iron, siderophores, and the pursuit of virulence: independence of the aerobactin and enterochelin iron uptake systems in Escherichia coli. Infect. Immun. 51, 942-947 (1986).
    • (1986) Infect. Immun. , vol.51 , pp. 942-947
    • Williams, P.H.1    Carbonetti, N.H.2
  • 24
    • 0036865552 scopus 로고    scopus 로고
    • The neutrophil lipocalin NGAL is a bacteriostatic agent that interferes with siderophore-mediated iron acquisition
    • Goetz, D.H. et al. The neutrophil lipocalin NGAL is a bacteriostatic agent that interferes with siderophore-mediated iron acquisition. Mol. Cell 10, 1033-1043 (2002).
    • (2002) Mol. Cell , vol.10 , pp. 1033-1043
    • Goetz, D.H.1
  • 25
    • 11844301598 scopus 로고    scopus 로고
    • Siderocalin (Lcn 2) also binds carboxymycobactins, potentially defending against mycobacterial infections through iron sequestration
    • Holmes, M.A., Paulsene, W., Jide, X., Ratledge, C. & Strong, R.K. Siderocalin (Lcn 2) also binds carboxymycobactins, potentially defending against mycobacterial infections through iron sequestration. Structure 13, 29-41 (2005).
    • (2005) Structure , vol.13 , pp. 29-41
    • Holmes, M.A.1    Paulsene, W.2    Jide, X.3    Ratledge, C.4    Strong, R.K.5
  • 26
    • 11144314814 scopus 로고    scopus 로고
    • Lipocalin 2 mediates an innate immune response to bacterial infection by sequestrating iron
    • Flo, T.H. et al. Lipocalin 2 mediates an innate immune response to bacterial infection by sequestrating iron. Nature 432, 917-921 (2004).
    • (2004) Nature , vol.432 , pp. 917-921
    • Flo, T.H.1
  • 27
    • 29244492306 scopus 로고    scopus 로고
    • A cell-surface receptor for lipocalin 24p3 selectively mediates apoptosis and iron uptake
    • Devireddy, L.R., Gazin, C., Zhu, X. & Green, M.R. A cell-surface receptor for lipocalin 24p3 selectively mediates apoptosis and iron uptake. Cell 123, 1293-1305 (2005).
    • (2005) Cell , vol.123 , pp. 1293-1305
    • Devireddy, L.R.1    Gazin, C.2    Zhu, X.3    Green, M.R.4
  • 28
    • 0035800508 scopus 로고    scopus 로고
    • Induction of apoptosis by a secreted lipocalin that is transcriptionally regulated by IL-3 deprivation
    • Devireddy, L.R., Teodora, J.G., Richard, F.A. & Green, M.R. Induction of apoptosis by a secreted lipocalin that is transcriptionally regulated by IL-3 deprivation. Science 293, 829-834 (2001).
    • (2001) Science , vol.293 , pp. 829-834
    • Devireddy, L.R.1    Teodora, J.G.2    Richard, F.A.3    Green, M.R.4
  • 29
    • 85029176042 scopus 로고    scopus 로고
    • Enzymatic tailoring of the bacterial siderophore enterobactin alters membrane partitioning and iron acquisition
    • in the press
    • Luo, M. et al. Enzymatic tailoring of the bacterial siderophore enterobactin alters membrane partitioning and iron acquisition. ACS Chem. Biol. (in the press).
    • ACS Chem. Biol.
    • Luo, M.1
  • 30
    • 0021265129 scopus 로고
    • Effect of serum albumin on siderophore-mediated utilization of transferrin iron
    • Konopka, K. & Neilands, J.B. Effect of serum albumin on siderophore-mediated utilization of transferrin iron. Biochemistry 23, 2122-2127 (1984).
    • (1984) Biochemistry , vol.23 , pp. 2122-2127
    • Konopka, K.1    Neilands, J.B.2
  • 31
    • 3042843855 scopus 로고    scopus 로고
    • The structure of salmochelins: C-glucosylated enterobactins of Salmonella enterica
    • Bister, B. et al. The structure of salmochelins: C-glucosylated enterobactins of Salmonella enterica. Biometals 17, 471-481 (2004).
    • (2004) Biometals , vol.17 , pp. 471-481
    • Bister, B.1
  • 32
    • 0141570419 scopus 로고    scopus 로고
    • Occurrence of the Yersinia high-pathogenicity island and iron uptake systems in clinical isolates of Klebsiella pneumoniae
    • Koczura, R. & Kaznowski, A. Occurrence of the Yersinia high-pathogenicity island and iron uptake systems in clinical isolates of Klebsiella pneumoniae. Microb. Pathog. 35, 197-202 (2003).
    • (2003) Microb. Pathog. , vol.35 , pp. 197-202
    • Koczura, R.1    Kaznowski, A.2
  • 33
    • 0030458858 scopus 로고    scopus 로고
    • Identification of a new iron regulated locus of Salmonella typhi
    • Baumler, A.J. et al. Identification of a new iron regulated locus of Salmonella typhi. Gene 183, 207-213 (1996).
    • (1996) Gene , vol.183 , pp. 207-213
    • Baumler, A.J.1
  • 34
    • 0031894919 scopus 로고    scopus 로고
    • IroN, a novel outer membrane siderophore receptor characteristic of Salmonella enterica
    • Baumler, A.J. et al. IroN, a novel outer membrane siderophore receptor characteristic of Salmonella enterica. J. Bacteriol. 180, 1446-1453 (1998).
    • (1998) J. Bacteriol. , vol.180 , pp. 1446-1453
    • Baumler, A.J.1
  • 35
    • 0026661296 scopus 로고
    • Effect of Salmonella typhimurium ferric uptake regulator (fur) mutations on iron- and pH-regulated protein synthesis
    • Foster, J.W. & Hall, H.K. Effect of Salmonella typhimurium ferric uptake regulator (fur) mutations on iron- and pH-regulated protein synthesis. J. Bacteriol. 174, 4317-4323 (1992).
    • (1992) J. Bacteriol. , vol.174 , pp. 4317-4323
    • Foster, J.W.1    Hall, H.K.2
  • 36
    • 0141814796 scopus 로고    scopus 로고
    • The colicin G, H and X determinants encode microcins M and H47, which might utilize the catecholate siderophore receptors FepA, Cir, Fiu and IroN
    • Patzer, S.I., Baquero, M.R., Bravo, D., Moreno, F. & Hantke, K. The colicin G, H and X determinants encode microcins M and H47, which might utilize the catecholate siderophore receptors FepA, Cir, Fiu and IroN. Microbiology 149, 2557-2570 (2003).
    • (2003) Microbiology , vol.149 , pp. 2557-2570
    • Patzer, S.I.1    Baquero, M.R.2    Bravo, D.3    Moreno, F.4    Hantke, K.5
  • 37
    • 0035950182 scopus 로고    scopus 로고
    • Complete genome sequence of Salmonella enterica serovar Typhimurium LT2
    • McClelland, M. et al. Complete genome sequence of Salmonella enterica serovar Typhimurium LT2. Nature 413, 852-856 (2001).
    • (2001) Nature , vol.413 , pp. 852-856
    • McClelland, M.1
  • 38
    • 0037168538 scopus 로고    scopus 로고
    • Extensive mosaic structure revealed by the complete genome sequence of uropathogenic Escherichia coli
    • Welch, R.A. et al. Extensive mosaic structure revealed by the complete genome sequence of uropathogenic Escherichia coli. Proc. Natl Acad. Sci. USA 99, 17020-17024 (2002).
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 17020-17024
    • Welch, R.A.1
  • 39
    • 3843116530 scopus 로고    scopus 로고
    • Analysis of the genome structure of the nonpathogenic probiotic Escherichia coli strain Nissle 1917
    • Grozdanov, L. et al. Analysis of the genome structure of the nonpathogenic probiotic Escherichia coli strain Nissle 1917. J. Bacteriol. 186, 5432-5441 (2004).
    • (2004) J. Bacteriol. , vol.186 , pp. 5432-5441
    • Grozdanov, L.1
  • 40
    • 0037470983 scopus 로고    scopus 로고
    • Role of mobile DNA in the evolution of vancomycin-resistant Enterococcus faecalis
    • Paulsen, I.T. et al. Role of mobile DNA in the evolution of vancomycin-resistant Enterococcus faecalis. Science 299, 2071-2074 (2003).
    • (2003) Science , vol.299 , pp. 2071-2074
    • Paulsen, I.T.1
  • 41
    • 0036841680 scopus 로고    scopus 로고
    • Genetic structure and distribution of four pathogenicity islands (PAI I(536) to PAI IV(536)) of uropathogenic Escherichia coli strain 536
    • Dobrindt, U. et al. Genetic structure and distribution of four pathogenicity islands (PAI I(536) to PAI IV(536)) of uropathogenic Escherichia coli strain 536. Infect. Immun. 70, 6365-6372 (2002).
    • (2002) Infect. Immun. , vol.70 , pp. 6365-6372
    • Dobrindt, U.1
  • 42
    • 0038781854 scopus 로고    scopus 로고
    • Characterization of an iroBCDEN gene cluster on a transmissible plasmid of uropathogenic Escherichia coli: Evidence for horizontal transfer of a chromosomal virulence factor
    • Sorsa, L.J., Dufke, S., Heesemann, J. & Schubert, S. Characterization of an iroBCDEN gene cluster on a transmissible plasmid of uropathogenic Escherichia coli: evidence for horizontal transfer of a chromosomal virulence factor. Infect. Immun. 71, 3285-3293 (2003).
    • (2003) Infect. Immun. , vol.71 , pp. 3285-3293
    • Sorsa, L.J.1    Dufke, S.2    Heesemann, J.3    Schubert, S.4
  • 43
    • 7044262987 scopus 로고    scopus 로고
    • Transcriptome of uropathogenic Escherichia coli during urinary tract infection
    • Snyder, J.A. et al. Transcriptome of uropathogenic Escherichia coli during urinary tract infection. Infect. Immun. 72, 6373-6381 (2004).
    • (2004) Infect. Immun. , vol.72 , pp. 6373-6381
    • Snyder, J.A.1
  • 44
    • 3242771398 scopus 로고    scopus 로고
    • Sequencing and analysis of the large virulence plasmid pLVPK of Klebsiella pneumoniae CG43
    • Chen, Y.T. et al. Sequencing and analysis of the large virulence plasmid pLVPK of Klebsiella pneumoniae CG43. Gene 337, 189-198 (2004).
    • (2004) Gene , vol.337 , pp. 189-198
    • Chen, Y.T.1
  • 45
    • 0035723807 scopus 로고    scopus 로고
    • Structure, organization and characterization of the gene cluster involved in the production of microcin E492, a channel-forming bacteriocin
    • Lagos, R. et al. Structure, organization and characterization of the gene cluster involved in the production of microcin E492, a channel-forming bacteriocin. Mol. Microbiol. 42, 229-243 (2001).
    • (2001) Mol. Microbiol. , vol.42 , pp. 229-243
    • Lagos, R.1
  • 46
    • 0027286543 scopus 로고
    • Expression of the ferric enterobactin receptor (PfeA) of Pseudomonas aeruginosa: Involvement of a two-component regulatory system
    • Dean, C.R. & Poole, K. Expression of the ferric enterobactin receptor (PfeA) of Pseudomonas aeruginosa: involvement of a two-component regulatory system. Mol. Microbiol. 8, 1095-1103 (1993).
    • (1993) Mol. Microbiol. , vol.8 , pp. 1095-1103
    • Dean, C.R.1    Poole, K.2
  • 47
    • 0037388150 scopus 로고    scopus 로고
    • Salmochelins, siderophores of Salmonella enterica and uropathogenic Escherichia coli strains, are recognized by the outer membrane receptor IroN
    • Hantke, K., Nicholson, G., Rabsch, W. & Winkelmann, G. Salmochelins, siderophores of Salmonella enterica and uropathogenic Escherichia coli strains, are recognized by the outer membrane receptor IroN. Proc. Natl Acad. Sci. USA 100, 3677-3682 (2003).
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 3677-3682
    • Hantke, K.1    Nicholson, G.2    Rabsch, W.3    Winkelmann, G.4
  • 48
    • 0038309565 scopus 로고    scopus 로고
    • Three monophyletic superfamilies account for the majority of the known glycosyltransferases
    • Liu, J. & Mushegian, A. Three monophyletic superfamilies account for the majority of the known glycosyltransferases. Protein Sci. 12, 1418-1431 (2003).
    • (2003) Protein Sci. , vol.12 , pp. 1418-1431
    • Liu, J.1    Mushegian, A.2
  • 49
    • 0042844760 scopus 로고    scopus 로고
    • Antibiotic glycosyltransferases: Antibiotic maturation and prospects for reprogramming
    • Walsh, C., Freel Meyers, C.L. & Losey, H.C. Antibiotic glycosyltransferases: antibiotic maturation and prospects for reprogramming. J. Med. Chem. 46, 3425-3436 (2003).
    • (2003) J. Med. Chem. , vol.46 , pp. 3425-3436
    • Walsh, C.1    Freel Meyers, C.L.2    Losey, H.C.3
  • 50
    • 14144253168 scopus 로고    scopus 로고
    • In vitro characterization of IroB, a pathogen-associated C-glycosyltransferase
    • Fischbach, M.A., Lin, H., Liu, D.R. & Walsh, C.T. In vitro characterization of IroB, a pathogen-associated C-glycosyltransferase. Proc. Natl Acad. Sci. USA 102, 571-576 (2005).
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 571-576
    • Fischbach, M.A.1    Lin, H.2    Liu, D.R.3    Walsh, C.T.4
  • 51
    • 0031127564 scopus 로고    scopus 로고
    • The role of carbohydrates in biologically active natural products
    • Weymouth-Wilson, A.C. The role of carbohydrates in biologically active natural products. Nat. Prod. Rep. 14, 99-110 (1997).
    • (1997) Nat. Prod. Rep. , vol.14 , pp. 99-110
    • Weymouth-Wilson, A.C.1
  • 52
    • 1642461379 scopus 로고    scopus 로고
    • Antimicrobial and DNA gyrase-inhibitory activities of novel clorobiocin derivatives produced by mutasynthesis
    • Galm, U. et al. Antimicrobial and DNA gyrase-inhibitory activities of novel clorobiocin derivatives produced by mutasynthesis. Antimicrob. Agents Chemother. 48, 1307-1312 (2004).
    • (2004) Antimicrob. Agents Chemother. , vol.48 , pp. 1307-1312
    • Galm, U.1
  • 53
    • 0035950132 scopus 로고    scopus 로고
    • Structural basis for the interaction of antibiotics with the peptidyl transferase centre in eubacteria
    • Schlunzen, F. et al. Structural basis for the interaction of antibiotics with the peptidyl transferase centre in eubacteria. Nature 413, 814-821 (2001).
    • (2001) Nature , vol.413 , pp. 814-821
    • Schlunzen, F.1
  • 54
    • 0037062576 scopus 로고    scopus 로고
    • DNA gyrase interaction with coumarin-based inhibitors: The role of the hydroxybenzoate isopentenyl moiety and the 5′-methyl group of the noviose
    • Lafitte, D. et al. DNA gyrase interaction with coumarin-based inhibitors: the role of the hydroxybenzoate isopentenyl moiety and the 5′-methyl group of the noviose. Biochemistry 41, 7217-7223 (2002).
    • (2002) Biochemistry , vol.41 , pp. 7217-7223
    • Lafitte, D.1
  • 56
    • 0031799094 scopus 로고    scopus 로고
    • Two glycosyltransferases and a glycosidase are involved in oleandomycin modification during its biosynthesis by Streptomyces antibioticus
    • Quiros, L.M., Aguirrezabalaga, I., Olano, C., Mendez, C. & Salas, J.A. Two glycosyltransferases and a glycosidase are involved in oleandomycin modification during its biosynthesis by Streptomyces antibioticus. Mol. Microbiol. 28, 1177-1185 (1998).
    • (1998) Mol. Microbiol. , vol.28 , pp. 1177-1185
    • Quiros, L.M.1    Aguirrezabalaga, I.2    Olano, C.3    Mendez, C.4    Salas, J.A.5
  • 58
    • 29244446754 scopus 로고    scopus 로고
    • Structure, activity, synthesis and biosynthesis of aryl-C-glycosides
    • Bililign, T., Griffith, B.R. & Thorson, J.S. Structure, activity, synthesis and biosynthesis of aryl-C-glycosides. Nat. Prod. Rep. 22, 742-760 (2005).
    • (2005) Nat. Prod. Rep. , vol.22 , pp. 742-760
    • Bililign, T.1    Griffith, B.R.2    Thorson, J.S.3
  • 59
    • 0034666159 scopus 로고    scopus 로고
    • Properdin, the positive regulator of complement, is highly C-mannosylated
    • Hartmann, S. & Hofsteenge, J. Properdin, the positive regulator of complement, is highly C-mannosylated. J. Biol. Chem. 275, 28569-28574 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 28569-28574
    • Hartmann, S.1    Hofsteenge, J.2
  • 60
    • 0032746280 scopus 로고    scopus 로고
    • The four terminal components of the complement system are C-mannosylated on multiple tryptophan residues
    • Hofsteenge, J., Blommers, M., Hess, D., Furmanek, A. & Miroshnichenko, O. The four terminal components of the complement system are C-mannosylated on multiple tryptophan residues. J. Biol. Chem. 274, 32786-32794 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 32786-32794
    • Hofsteenge, J.1    Blommers, M.2    Hess, D.3    Furmanek, A.4    Miroshnichenko, O.5
  • 61
    • 1842413048 scopus 로고    scopus 로고
    • C-Mannosylation of human RNase 2 is an intracellular process performed by a variety of cultured cells
    • Krieg, J. et al. C-Mannosylation of human RNase 2 is an intracellular process performed by a variety of cultured cells. J. Biol. Chem. 272, 26687-26692 (1997).
    • (1997) J. Biol. Chem. , vol.272 , pp. 26687-26692
    • Krieg, J.1
  • 62
    • 2442519149 scopus 로고    scopus 로고
    • C-Mannosylation of MUC5AC and MUC5B Cys subdomains
    • Perez-Vilar, J., Randell, S.H. & Boucher, R.C. C-Mannosylation of MUC5AC and MUC5B Cys subdomains. Glycobiology 14, 325-337 (2004).
    • (2004) Glycobiology , vol.14 , pp. 325-337
    • Perez-Vilar, J.1    Randell, S.H.2    Boucher, R.C.3
  • 63
    • 17444449236 scopus 로고    scopus 로고
    • Function of glycosyltransferase genes involved in urdamycin A biosynthesis
    • Trefzer, A. et al. Function of glycosyltransferase genes involved in urdamycin A biosynthesis. Chem. Biol. 7, 133-142 (2000).
    • (2000) Chem. Biol. , vol.7 , pp. 133-142
    • Trefzer, A.1
  • 64
    • 0032478297 scopus 로고    scopus 로고
    • Quantitative trait loci and metabolic pathways
    • McMullen, M.D. et al. Quantitative trait loci and metabolic pathways. Proc. Natl Acad. Sci. USA 95, 1996-2000 (1998).
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 1996-2000
    • McMullen, M.D.1
  • 65
    • 22144439383 scopus 로고    scopus 로고
    • Functions of the siderophore esterases IroD and IroE in iron-salmochelin utilization
    • Zhu, M., Valdebenito, M., Winkelmann, G. & Hantke, K. Functions of the siderophore esterases IroD and IroE in iron-salmochelin utilization. Microbiology 151, 2363-2372 (2005).
    • (2005) Microbiology , vol.151 , pp. 2363-2372
    • Zhu, M.1    Valdebenito, M.2    Winkelmann, G.3    Hantke, K.4
  • 66
    • 13644264724 scopus 로고    scopus 로고
    • Membrane dynamics of the amphiphilic siderophore, acinetoferrin
    • Luo, M., Fadeev, E.A. & Groves, J.T. Membrane dynamics of the amphiphilic siderophore, acinetoferrin. J. Am. Chem. Soc. 127, 1726-1736 (2005).
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 1726-1736
    • Luo, M.1    Fadeev, E.A.2    Groves, J.T.3
  • 67
    • 0029839633 scopus 로고    scopus 로고
    • The occurrence of carboxymycobactin, the siderophore of pathogenic mycobacteria, as a second extracellular siderophore in Mycobacterium smegmatis
    • Ratledge, C. & Ewing, M. The occurrence of carboxymycobactin, the siderophore of pathogenic mycobacteria, as a second extracellular siderophore in Mycobacterium smegmatis. Microbiology 142, 2207-2212 (1996).
    • (1996) Microbiology , vol.142 , pp. 2207-2212
    • Ratledge, C.1    Ewing, M.2
  • 68
    • 0036589245 scopus 로고    scopus 로고
    • Focus on modified microcins: Structural features and mechanisms of action
    • Destoumieux-Garzon, D., Peduzzi, J. & Rebuffat, S. Focus on modified microcins: structural features and mechanisms of action. Biochimie 84, 511-519 (2002).
    • (2002) Biochimie , vol.84 , pp. 511-519
    • Destoumieux-Garzon, D.1    Peduzzi, J.2    Rebuffat, S.3
  • 69
    • 0029923954 scopus 로고    scopus 로고
    • From peptide precursors to oxazole and thiazole-containing peptide antibiotics: Microcin B17 synthase
    • Li, Y.M., Milne, J.C., Madison, L.L., Kolter, R. & Walsh, C.T. From peptide precursors to oxazole and thiazole-containing peptide antibiotics: microcin B17 synthase. Science 274, 1188-1193 (1996).
    • (1996) Science , vol.274 , pp. 1188-1193
    • Li, Y.M.1    Milne, J.C.2    Madison, L.L.3    Kolter, R.4    Walsh, C.T.5
  • 70
    • 0141988966 scopus 로고    scopus 로고
    • Structure of antibacterial peptide microcin J25: A 21-residue lariat protoknot
    • Bayro, M.J. et al. Structure of antibacterial peptide microcin J25: a 21-residue lariat protoknot. J. Am. Chem. Soc. 125, 12382-12383 (2003).
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 12382-12383
    • Bayro, M.J.1
  • 71
    • 0141919822 scopus 로고    scopus 로고
    • Microcin J25 has a threaded sidechain-to-backbone ring structure and not a head-to-tail cyclized backbone
    • Rosengren, K.J. et al. Microcin J25 has a threaded sidechain-to-backbone ring structure and not a head-to-tail cyclized backbone. J. Am. Chem. Soc. 125, 12464-12474 (2003).
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 12464-12474
    • Rosengren, K.J.1
  • 72
    • 18944379638 scopus 로고    scopus 로고
    • Structure-activity analysis of microcinJ25: Distinct parts of the threaded lasso molecule are responsible for interaction with bacterial RNA polymerase
    • Semenova, E., Yuzenkova, Y., Peduzzi, J., Rebuffat, S. & Severinov, K. Structure-activity analysis of microcinJ25: distinct parts of the threaded lasso molecule are responsible for interaction with bacterial RNA polymerase. J. Bacteriol. 187, 3859-3863 (2005).
    • (2005) J. Bacteriol. , vol.187 , pp. 3859-3863
    • Semenova, E.1    Yuzenkova, Y.2    Peduzzi, J.3    Rebuffat, S.4    Severinov, K.5
  • 73
    • 0141919821 scopus 로고    scopus 로고
    • Structure of microcin J25, a peptide inhibitor of bacterial RNA polymerase, is a lassoed tail
    • Wilson, K.A. et al. Structure of microcin J25, a peptide inhibitor of bacterial RNA polymerase, is a lassoed tail. J. Am. Chem. Soc. 125, 12475-12483 (2003).
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 12475-12483
    • Wilson, K.A.1
  • 74
    • 0027533645 scopus 로고
    • Microcin E492 forms ion channels in phospholipid bilayer membrane
    • Lagos, R., Wilkens, M., Vergara, C., Cecchi, X. & Monasterio, O. Microcin E492 forms ion channels in phospholipid bilayer membrane. FEBS Lett. 321, 145-148 (1993).
    • (1993) FEBS Lett. , vol.321 , pp. 145-148
    • Lagos, R.1    Wilkens, M.2    Vergara, C.3    Cecchi, X.4    Monasterio, O.5
  • 75
    • 3142543798 scopus 로고    scopus 로고
    • Siderophore peptide, a new type of post-translationally modified antibacterial peptide with potent activity
    • Thomas, X. et al. Siderophore peptide, a new type of post-translationally modified antibacterial peptide with potent activity. J. Biol. Chem. 279, 28233-28242 (2004).
    • (2004) J. Biol. Chem. , vol.279 , pp. 28233-28242
    • Thomas, X.1
  • 76
    • 0032947987 scopus 로고    scopus 로고
    • Identification and properties of the genes encoding microcin E492 and its immunity protein
    • Lagos, R., Villanueva, J.E. & Monasterio, O. Identification and properties of the genes encoding microcin E492 and its immunity protein. J. Bacteriol. 181, 212-217 (1999).
    • (1999) J. Bacteriol. , vol.181 , pp. 212-217
    • Lagos, R.1    Villanueva, J.E.2    Monasterio, O.3
  • 77
    • 21444438149 scopus 로고    scopus 로고
    • Cooperative uptake of microcin E492 by receptors FepA, Fiu, and Cir and inhibition by the siderophore enterochelin and its dimeric and trimeric hydrolysis products
    • Strahsburger, E., Baeza, M., Monasterio, O. & Lagos, R. Cooperative uptake of microcin E492 by receptors FepA, Fiu, and Cir and inhibition by the siderophore enterochelin and its dimeric and trimeric hydrolysis products. Antimicrob. Agents Chemother. 49, 3083-3086 (2005).
    • (2005) Antimicrob. Agents Chemother. , vol.49 , pp. 3083-3086
    • Strahsburger, E.1    Baeza, M.2    Monasterio, O.3    Lagos, R.4
  • 78
    • 0032720091 scopus 로고    scopus 로고
    • Ferric enterochelin transport in Yersinia enterocolitica: Molecular and evolutionary aspects
    • Schubert, S., Fischer, D. & Heesemann, J. Ferric enterochelin transport in Yersinia enterocolitica: molecular and evolutionary aspects. J. Bacteriol. 181, 6387-6395 (1999).
    • (1999) J. Bacteriol. , vol.181 , pp. 6387-6395
    • Schubert, S.1    Fischer, D.2    Heesemann, J.3
  • 79
    • 0036233610 scopus 로고    scopus 로고
    • Biosynthetic gene cluster of simocyclinone, a natural multihybrid antibiotic
    • Trefzer, A. et al. Biosynthetic gene cluster of simocyclinone, a natural multihybrid antibiotic. Antimicrob. Agents Chemother. 46, 1174-1182 (2002).
    • (2002) Antimicrob. Agents Chemother. , vol.46 , pp. 1174-1182
    • Trefzer, A.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.