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Volumn 84, Issue 1-2, 2004, Pages 110-130

Iron, mycobacteria and tuberculosis

Author keywords

Bacterioferritin; Carboxymycobactin; Disease management; Exochelin; Inhibitors; Mycobactin; PAS; Salicylic acid; Siderophores; Tuberculosis

Indexed keywords

4 AMINOBENZOIC ACID; AMINOSALICYLIC ACID; APOPROTEIN; BACTERIOFERRITIN; CARBOXYMYCOBACTIN; EXOCHELIN; FERRIC ION; FERRITIN; FERROUS ION; IRON DERIVATIVE; LACTOFERRIN; MYCOBACTIN; OXIDOREDUCTASE; PORPHYRIN; SALICYLIC ACID; SIDEROPHORE; TRANSFERRIN; TUBERCULOSTATIC AGENT; UNCLASSIFIED DRUG;

EID: 0347722524     PISSN: 14729792     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tube.2003.08.012     Document Type: Conference Paper
Times cited : (290)

References (109)
  • 2
    • 0035069457 scopus 로고    scopus 로고
    • Iron and metal regulation in bacteria
    • Hantke K. Iron and metal regulation in bacteria. Curr Opin Microbiol 2001;4:172-7.
    • (2001) Curr Opin Microbiol , vol.4 , pp. 172-177
    • Hantke, K.1
  • 3
    • 0033759220 scopus 로고    scopus 로고
    • Iron metabolism in pathogenic bacteria
    • Ratledge C, Dover LG. Iron metabolism in pathogenic bacteria. Annu Rev Microbiol 2000;54:881-941.
    • (2000) Annu Rev Microbiol , vol.54 , pp. 881-941
    • Ratledge, C.1    Dover, L.G.2
  • 5
    • 0027435537 scopus 로고
    • Iron uptake mechanisms in pathogenic bacteria
    • Woodridge KG, Williams PH. Iron uptake mechanisms in pathogenic bacteria. FEMS Microbiol Rev 1993;12:325-48.
    • (1993) FEMS Microbiol Rev , vol.12 , pp. 325-348
    • Woodridge, K.G.1    Williams, P.H.2
  • 7
    • 0001833804 scopus 로고    scopus 로고
    • Iron metabolism
    • Ratledge C, Dale J, editors. Oxford, UK: Blackwell Science
    • Ratledge C. Iron metabolism. In: Ratledge C, Dale J, editors. Mycobacteria: molecular biology and virulence. Oxford, UK: Blackwell Science; 1999. p. 206-86.
    • (1999) Mycobacteria: Molecular Biology and Virulence , pp. 206-286
    • Ratledge, C.1
  • 8
    • 0034458643 scopus 로고    scopus 로고
    • Iron as a candidate in virulence and pathogenesis in mycobacteria and other organisms
    • Sritharan M. Iron as a candidate in virulence and pathogenesis in mycobacteria and other organisms. World J Microbiol Biotechnol 2000;16:769-80.
    • (2000) World J Microbiol Biotechnol , vol.16 , pp. 769-780
    • Sritharan, M.1
  • 9
    • 0002919912 scopus 로고    scopus 로고
    • Determinants of mycobacterial gene expression
    • Hatfull GF, Jacobs WR, editors. Washington, DC: American Society for Microbiology Press
    • Gomez M, Smith I. Determinants of mycobacterial gene expression. In: Hatfull GF, Jacobs WR, editors. Molecular genetics of mycobacteria. Washington, DC: American Society for Microbiology Press; 2000. p. 111-29.
    • (2000) Molecular Genetics of Mycobacteria , pp. 111-129
    • Gomez, M.1    Smith, I.2
  • 10
    • 0002983079 scopus 로고    scopus 로고
    • Cell wall: Physical structure and permeability
    • Ratledge C, Dale JW, editors. Oxford, UK: Blackwell Sciences
    • Liu J, Barry III CE, Nikaido H. Cell wall: physical structure and permeability. In: Ratledge C, Dale JW, editors. Mycobacteria molecular biology and virulence. Oxford, UK: Blackwell Sciences; 1999. p. 220-39.
    • (1999) Mycobacteria Molecular Biology and Virulence , pp. 220-239
    • Liu, J.1    Barry III, C.E.2    Nikaido, H.3
  • 11
    • 0033811814 scopus 로고    scopus 로고
    • Salicylate is not a bacterial siderophore: A theoretical study
    • Chipperfield JR, Ratledge C. Salicylate is not a bacterial siderophore: a theoretical study. Biometals 2000;13:165-8.
    • (2000) Biometals , vol.13 , pp. 165-168
    • Chipperfield, J.R.1    Ratledge, C.2
  • 16
    • 0032997261 scopus 로고    scopus 로고
    • Iron loading and disease surveillance
    • Weinberg ED. Iron loading and disease surveillance. Emerging Infect Dis 1999;5:346-52.
    • (1999) Emerging Infect Dis , vol.5 , pp. 346-352
    • Weinberg, E.D.1
  • 17
    • 0345943229 scopus 로고    scopus 로고
    • Therapeutic potential of human transferring and lactoferrin
    • Weinberg ED. Therapeutic potential of human transferring and lactoferrin. ASM News 2002;68:65-9.
    • (2002) ASM News , vol.68 , pp. 65-69
    • Weinberg, E.D.1
  • 18
    • 0015543357 scopus 로고
    • Role of iron in bacterial infections with special consideration to host-tubercle bacillus interaction
    • Kochan I. Role of iron in bacterial infections with special consideration to host-tubercle bacillus interaction. Curr Top Microbiol Immun 1973;60:1-30.
    • (1973) Curr Top Microbiol Immun , vol.60 , pp. 1-30
    • Kochan, I.1
  • 19
    • 0022765788 scopus 로고
    • Participation of iron in the growth inhibition of pathogenic strains of Mycobacterium avium and Mycobacterium paratuberculosis in serum
    • Barclay R, Ratledge C. Participation of iron in the growth inhibition of pathogenic strains of Mycobacterium avium and Mycobacterium paratuberculosis in serum. Z Bakt Mikrobiol Hyg 1986;A262:189-94.
    • (1986) Z Bakt Mikrobiol Hyg , vol.A262 , pp. 189-194
    • Barclay, R.1    Ratledge, C.2
  • 20
    • 0029913805 scopus 로고    scopus 로고
    • Exochelins of Mycobacterium tuberculosis remove iron from human iron-binding proteins and donate iron to mycobactins in the Mycobacterium tuberculosis cell wall
    • Gobin J, Horwitz MA. Exochelins of Mycobacterium tuberculosis remove iron from human iron-binding proteins and donate iron to mycobactins in the Mycobacterium tuberculosis cell wall. J Exp Med 1996;183:1527-32.
    • (1996) J Exp Med , vol.183 , pp. 1527-1532
    • Gobin, J.1    Horwitz, M.A.2
  • 21
    • 0027411035 scopus 로고
    • Transferrin, iron, and serum lipids enhance or inhibit Mycobacterium avium replication in human macrophages
    • Douvas GS, May MH, Crowle AJ. Transferrin, iron, and serum lipids enhance or inhibit Mycobacterium avium replication in human macrophages. J Infect Dis 1993;167: 857-64.
    • (1993) J Infect Dis , vol.167 , pp. 857-864
    • Douvas, G.S.1    May, M.H.2    Crowle, A.J.3
  • 27
    • 0014803645 scopus 로고
    • Mycobactins: Iron-chelating growth factors from mycobacteria
    • Snow GA. Mycobactins: iron-chelating growth factors from mycobacteria. Bacteriol Rev 1970;34:99-125.
    • (1970) Bacteriol Rev , vol.34 , pp. 99-125
    • Snow, G.A.1
  • 28
    • 0020540519 scopus 로고
    • Iron-binding compounds of Mycobacterium, Mycobacterium scrofulaceum and mycobactin-dependent Mycobacterium paratuberculosis and Mycobacterium avium
    • Barclay R, Ratledge C. Iron-binding compounds of Mycobacterium, Mycobacterium scrofulaceum and mycobactin-dependent Mycobacterium paratuberculosis and Mycobacterium avium. J Bacteriol 1983;153:1138-46.
    • (1983) J Bacteriol , vol.153 , pp. 1138-1146
    • Barclay, R.1    Ratledge, C.2
  • 29
    • 0026641775 scopus 로고
    • A simple and rapid method for the detection and identification of mycobacteria using mycobactin
    • Barclay R, Furst V, Smith I. A simple and rapid method for the detection and identification of mycobacteria using mycobactin. J Med Microbiol 1992;37:286-90.
    • (1992) J Med Microbiol , vol.37 , pp. 286-290
    • Barclay, R.1    Furst, V.2    Smith, I.3
  • 30
    • 0026575523 scopus 로고
    • Mycobactin analysis as an aid for the identification of Mycobacterium fortuitum and Mycobacterium chelonae subspecies
    • Bosne S, Levy-Frebault W. Mycobactin analysis as an aid for the identification of Mycobacterium fortuitum and Mycobacterium chelonae subspecies. J Clin Microbiol 1992;30: 1225-31.
    • (1992) J Clin Microbiol , vol.30 , pp. 1225-1231
    • Bosne, S.1    Levy-Frebault, W.2
  • 31
    • 0008935138 scopus 로고
    • Mycobactins: How to obtain them and how to employ them as chemotaxonomic characters for the mycobacteria and related organisms
    • Hall RM. Mycobactins: how to obtain them and how to employ them as chemotaxonomic characters for the mycobacteria and related organisms. Actinomycetes 1986;19:92-106.
    • (1986) Actinomycetes , vol.19 , pp. 92-106
    • Hall, R.M.1
  • 32
    • 0021222459 scopus 로고
    • Mycobactins as chemotaxonomic characters for some rapidly growing mycobacteria
    • Hall RM, Ratledge C. Mycobactins as chemotaxonomic characters for some rapidly growing mycobacteria. J Gen Microbiol 1984;130:1883-92.
    • (1984) J Gen Microbiol , vol.130 , pp. 1883-1892
    • Hall, R.M.1    Ratledge, C.2
  • 33
    • 0008938372 scopus 로고
    • TLC of mycobactins and mycolic acid for the identification of clinical mycobacteria
    • Leite CQF, Barreto AMW, Leite SRA. TLC of mycobactins and mycolic acid for the identification of clinical mycobacteria. Rev Microbiol (Sao Paulo) 1995;26:192-9.
    • (1995) Rev Microbiol (Sao Paulo) , vol.26 , pp. 192-199
    • Leite, C.Q.F.1    Barreto, A.M.W.2    Leite, S.R.A.3
  • 34
    • 0025022083 scopus 로고
    • Iron-regulated envelope proteins of mycobacteria grown in vitro and their occurrence in Mycobacterium avium and Mycobacterium leprae grown in vivo
    • Sritharan M, Ratledge C. Iron-regulated envelope proteins of mycobacteria grown in vitro and their occurrence in Mycobacterium avium and Mycobacterium leprae grown in vivo. Biol Met 1990;2:203-8.
    • (1990) Biol Met , vol.2 , pp. 203-208
    • Sritharan, M.1    Ratledge, C.2
  • 35
    • 0027223487 scopus 로고
    • Inability to detect mycobactin in mycobacteria infected tissues suggests an alternative iron acquisition mechanism by mycobacteria in vivo
    • Lambrecht RS, Collins MT. Inability to detect mycobactin in mycobacteria infected tissues suggests an alternative iron acquisition mechanism by mycobacteria in vivo. Microb Pathog 1993;14:229-38.
    • (1993) Microb Pathog , vol.14 , pp. 229-238
    • Lambrecht, R.S.1    Collins, M.T.2
  • 36
    • 0033973479 scopus 로고    scopus 로고
    • The salicylate-derived mycobacteria siderophores of Mycobacterium tuberculosis are essential for growth in microphages
    • De Voss JJ, Rutter K, Schroeder BG, Su H, Zhu YQ, Barry III CE. The salicylate-derived mycobacteria siderophores of Mycobacterium tuberculosis are essential for growth in microphages. Proc Natl Acad Sci USA 2000;97:1252-7.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 1252-1257
    • De Voss, J.J.1    Rutter, K.2    Schroeder, B.G.3    Su, H.4    Zhu, Y.Q.5    Barry III, C.E.6
  • 37
    • 0036263753 scopus 로고    scopus 로고
    • Use of an assayed promotor-probe library for the identification of macrophage-regulated genes in Mycobacterium tuberculosis
    • Hobson RJ, McBride AJA, Kempsell KE, Dale JW. Use of an assayed promotor-probe library for the identification of macrophage-regulated genes in Mycobacterium tuberculosis. Microbiology 2002;148:1571-9.
    • (2002) Microbiology , vol.148 , pp. 1571-1579
    • Hobson, R.J.1    McBride, A.J.A.2    Kempsell, K.E.3    Dale, J.W.4
  • 38
    • 0001544469 scopus 로고
    • The accumulation of salicylic acid by mycobacteria during growth on iron-deficient medium
    • Ratledge C, Winder FG. The accumulation of salicylic acid by mycobacteria during growth on iron-deficient medium. Biochem J 1962;84:501-6.
    • (1962) Biochem J , vol.84 , pp. 501-506
    • Ratledge, C.1    Winder, F.G.2
  • 39
    • 0026601590 scopus 로고
    • Isolation of a novel siderophore from Pseudomonas cepacia
    • Sokol PA, Lewis CJ, Dennis JJ. Isolation of a novel siderophore from Pseudomonas cepacia. J Med Microbiol 1992;36:184-9.
    • (1992) J Med Microbiol , vol.36 , pp. 184-189
    • Sokol, P.A.1    Lewis, C.J.2    Dennis, J.J.3
  • 40
    • 0027484113 scopus 로고
    • Iron-regulated salicylate synthesis by Pseudomonas spp.
    • Visca P, Ciervo A, Sanfilippo V, Orsi N. Iron-regulated salicylate synthesis by Pseudomonas spp. J Gen Microbiol 1993;139:1995-2001.
    • (1993) J Gen Microbiol , vol.139 , pp. 1995-2001
    • Visca, P.1    Ciervo, A.2    Sanfilippo, V.3    Orsi, N.4
  • 41
    • 0016261005 scopus 로고
    • Iron transport in Mycobacterium smegmatis: A restricted role for salicylic acid in the extracellular environment
    • Ratledge C, Macham LP, Brown KA, Marshall BJ. Iron transport in Mycobacterium smegmatis: a restricted role for salicylic acid in the extracellular environment. Biochim Biophys Acta 1974;372:39-51.
    • (1974) Biochim Biophys Acta , vol.372 , pp. 39-51
    • Ratledge, C.1    Macham, L.P.2    Brown, K.A.3    Marshall, B.J.4
  • 42
    • 0016774173 scopus 로고
    • A new group of water-soluble iron-binding compounds from mycobacteria: The exochelins
    • Macham LP, Ratledge C. A new group of water-soluble iron-binding compounds from mycobacteria: the exochelins. J Gen Microbiol 1975;89:379-82.
    • (1975) J Gen Microbiol , vol.89 , pp. 379-382
    • Macham, L.P.1    Ratledge, C.2
  • 43
    • 0016790996 scopus 로고
    • Extracellular iron acquisition by mycobacteria: Role of the exochelins and evidence against the participation of mycobactin
    • Macham LP, Ratledge C, Nocton JC. Extracellular iron acquisition by mycobacteria: role of the exochelins and evidence against the participation of mycobactin. Infect Immun 1975;12:1242-51.
    • (1975) Infect Immun , vol.12 , pp. 1242-1251
    • Macham, L.P.1    Ratledge, C.2    Nocton, J.C.3
  • 44
    • 0028854121 scopus 로고
    • Isolation purification and structure of exochelin MS, the extracellular siderophore from Mycobacterium smegmatis
    • Sharman GJ, Williams DH, Ewing DF, Ratledge C. Isolation purification and structure of exochelin MS, the extracellular siderophore from Mycobacterium smegmatis. Biochem J 1995;305:187-96.
    • (1995) Biochem J , vol.305 , pp. 187-196
    • Sharman, G.J.1    Williams, D.H.2    Ewing, D.F.3    Ratledge, C.4
  • 45
    • 0029347184 scopus 로고
    • Determination of the structure of exochelin MN, the extracellular Mycobacterium neoaurum
    • Sharman GJ, Williams DH, Ewing DF, Ratledge C. Determination of the structure of exochelin MN, the extracellular Mycobacterium neoaurum. Chem Biol 1995;2:553-61.
    • (1995) Chem Biol , vol.2 , pp. 553-561
    • Sharman, G.J.1    Williams, D.H.2    Ewing, D.F.3    Ratledge, C.4
  • 46
    • 0028999977 scopus 로고
    • Iron acquisition by Mycobacterium tuberculosis: Isolation and characterization of a family of iron-binding exochelins
    • Gobin J, Moore CH, Reeve Jr JR, Wong DK, Gibson BW, Horwitz MA. Iron acquisition by Mycobacterium tuberculosis: isolation and characterization of a family of iron-binding exochelins. Proc Natl Acad Sci USA 1995;92: 5189-93.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 5189-5193
    • Gobin, J.1    Moore, C.H.2    Reeve Jr., J.R.3    Wong, D.K.4    Gibson, B.W.5    Horwitz, M.A.6
  • 47
    • 0029058855 scopus 로고
    • Novel extracellular mycobactins, the carboxymycobactins from Mycobacterium avium
    • Lane SJ, Marshall PS, Upton RJ, Ratledge C, Ewing M. Novel extracellular mycobactins, the carboxymycobactins from Mycobacterium avium. Tetrahedron Lett 1995;36: 4129-32.
    • (1995) Tetrahedron Lett , vol.36 , pp. 4129-4132
    • Lane, S.J.1    Marshall, P.S.2    Upton, R.J.3    Ratledge, C.4    Ewing, M.5
  • 48
    • 0033986292 scopus 로고    scopus 로고
    • Mutational analysis of a role for salicylic acid in iron metabolism of Mycobocterium smegmatis
    • Adilakshmi T, Ayling PD, Ratledge C. Mutational analysis of a role for salicylic acid in iron metabolism of Mycobocterium smegmatis. J Bacteriol 2000;182:264-71.
    • (2000) J Bacteriol , vol.182 , pp. 264-271
    • Adilakshmi, T.1    Ayling, P.D.2    Ratledge, C.3
  • 49
    • 0033047175 scopus 로고    scopus 로고
    • Characterization of exochelins of the Mycobacterium bovis type strain and BCG substrains
    • Gobin J, Wong DK, Gibson BW, Horwitz MA. Characterization of exochelins of the Mycobacterium bovis type strain and BCG substrains. Infect Immun 1999;67:2035-9.
    • (1999) Infect Immun , vol.67 , pp. 2035-2039
    • Gobin, J.1    Wong, D.K.2    Gibson, B.W.3    Horwitz, M.A.4
  • 50
    • 0031820390 scopus 로고    scopus 로고
    • Exochelin genes in Mycobacterium smegmatis: Identification of an ABC transporter and two nonribosomal peptide synthetase genes
    • Zhu W, Arceneaux JEL, Beggs ML, Eisenbach KD, Ludrigan MD. Exochelin genes in Mycobacterium smegmatis: identification of an ABC transporter and two nonribosomal peptide synthetase genes. Mol Microbiol 1998;29:629-39.
    • (1998) Mol Microbiol , vol.29 , pp. 629-639
    • Zhu, W.1    Arceneaux, J.E.L.2    Beggs, M.L.3    Eisenbach, K.D.4    Ludrigan, M.D.5
  • 51
    • 0031975757 scopus 로고    scopus 로고
    • Isolation and characterisation of carboxymycobactin as the second extracellular siderophore in Mycobacterium smegmatis
    • Lane SJ, Marshall PS, Upton RJ, Ratledge C. Isolation and characterisation of carboxymycobactin as the second extracellular siderophore in Mycobacterium smegmatis. Biometals 1998;11:13-20.
    • (1998) Biometals , vol.11 , pp. 13-20
    • Lane, S.J.1    Marshall, P.S.2    Upton, R.J.3    Ratledge, C.4
  • 52
    • 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 1996;142:2207-12.
    • (1996) Microbiology , vol.142 , pp. 2207-2212
    • Ratledge, C.1    Ewing, M.2
  • 53
    • 0018372996 scopus 로고
    • Iron transport in Mycobacterium smegmatis: Uptake of iron from ferriexochelin
    • Stephenson MC, Ratledge C. Iron transport in Mycobacterium smegmatis: uptake of iron from ferriexochelin. J Gen Microbiol 1979;110:193-202.
    • (1979) J Gen Microbiol , vol.110 , pp. 193-202
    • Stephenson, M.C.1    Ratledge, C.2
  • 54
    • 0028127357 scopus 로고
    • Identification of genes involved in the sequestration of iron in mycobacteria: The ferric exochelin biosynthetic and uptake pathways
    • Fiss EH, Yu S, Jacobs WR. Identification of genes involved in the sequestration of iron in mycobacteria: the ferric exochelin biosynthetic and uptake pathways. Mol Microbiol 1994;14:557-69.
    • (1994) Mol Microbiol , vol.14 , pp. 557-569
    • Fiss, E.H.1    Yu, S.2    Jacobs, W.R.3
  • 55
    • 0031783529 scopus 로고    scopus 로고
    • Analysis of the exochelin locus in Mycobacterium smegmatis: Biosynthesis genes have homology with genes of the peptide synthetase family
    • Yu S, Fiss E, Jacobs WR. Analysis of the exochelin locus in Mycobacterium smegmatis: biosynthesis genes have homology with genes of the peptide synthetase family. J Bacteriol 1998;180:4676-85.
    • (1998) J Bacteriol , vol.180 , pp. 4676-4685
    • Yu, S.1    Fiss, E.2    Jacobs, W.R.3
  • 56
    • 0023388769 scopus 로고
    • Iron transport in Mycobacterium smegmotis: Occurrence of iron-regulated envelope proteins as potential receptors for iron uptake
    • Hall RM, Sritharan M, Messenger AJM, Ratledge C. Iron transport in Mycobacterium smegmotis: occurrence of iron-regulated envelope proteins as potential receptors for iron uptake. J Gen Microbiol 1987;133:2107-14.
    • (1987) J Gen Microbiol , vol.133 , pp. 2107-2114
    • Hall, R.M.1    Sritharan, M.2    Messenger, A.J.M.3    Ratledge, C.4
  • 57
    • 0029896844 scopus 로고    scopus 로고
    • Identification of a 29kDa protein in the envelope of Mycobacterium smegmatis as a putative ferri-exochelin receptor
    • Dover LG, Ratledge C. Identification of a 29kDa protein in the envelope of Mycobacterium smegmatis as a putative ferri-exochelin receptor. Microbiology 1996;142:1521-30.
    • (1996) Microbiology , vol.142 , pp. 1521-1530
    • Dover, L.G.1    Ratledge, C.2
  • 58
    • 0012949783 scopus 로고    scopus 로고
    • Genetics of mycobacterial metabolism
    • Hatfull GF, Jacobs Jr WR, editors. Washington, DC: American Society for Microbiology
    • Pavelka Jr. MS. Genetics of mycobacterial metabolism. In: Hatfull GF, Jacobs Jr WR, editors. Molecular genetics of mycobacteria. Washington, DC: American Society for Microbiology; 2000. p. 221-34.
    • (2000) Molecular Genetics of Mycobacteria , pp. 221-234
    • Pavelka Jr., M.S.1
  • 59
    • 0018898554 scopus 로고
    • Specificity of exochelins for iron transport in three species of mycobacteria
    • Stephenson MC, Ratledge C. Specificity of exochelins for iron transport in three species of mycobacteria. J Gen Microbiol 1980;116:521-3.
    • (1980) J Gen Microbiol , vol.116 , pp. 521-523
    • Stephenson, M.C.1    Ratledge, C.2
  • 60
    • 0028113382 scopus 로고
    • Permeability of the cell wall of Mycobacterium smegmatis
    • Trias J, Benz R. Permeability of the cell wall of Mycobacterium smegmatis. Mol Microbiol 1994;14:283-90.
    • (1994) Mol Microbiol , vol.14 , pp. 283-290
    • Trias, J.1    Benz, R.2
  • 61
    • 0027064590 scopus 로고
    • Porins in the cell wall of mycobacteria
    • Trias J, Jarlier V, Benz R. Porins in the cell wall of mycobacteria. Science 1992;258:1479-81.
    • (1992) Science , vol.258 , pp. 1479-1481
    • Trias, J.1    Jarlier, V.2    Benz, R.3
  • 62
    • 0015949901 scopus 로고
    • The crystal structure of ferrimycobactin P, a growth factor for the mycobacteria
    • Hough E, Rogers D. The crystal structure of ferrimycobactin P, a growth factor for the mycobacteria. Biochem Biophys Res Commun 1974;57:73-7.
    • (1974) Biochem Biophys Res Commun , vol.57 , pp. 73-77
    • Hough, E.1    Rogers, D.2
  • 63
    • 0031932979 scopus 로고    scopus 로고
    • Identification of iron-regulated proteins of Mycobacterium tuberculosis and cloning of tandem genes encoding a low-iron-induced protein and a metal transporting ATPase with similarities to two-component metal transport systems
    • Calder KM, Horwitz MA. Identification of iron-regulated proteins of Mycobacterium tuberculosis and cloning of tandem genes encoding a low-iron-induced protein and a metal transporting ATPase with similarities to two-component metal transport systems. Microb Pathog 1998;24: 133-43.
    • (1998) Microb Pathog , vol.24 , pp. 133-143
    • Calder, K.M.1    Horwitz, M.A.2
  • 64
    • 0016782768 scopus 로고
    • Iron transport in Mycobacterium smegmatis: Ferrimycobactin reductase (NAD(P)H: Ferrimycobactin oxidoreductase), the enzyme releasing iron from its carrier
    • Brown KA, Ratledge C. Iron transport in Mycobacterium smegmatis: ferrimycobactin reductase (NAD(P)H: ferrimycobactin oxidoreductase), the enzyme releasing iron from its carrier. FEBS Lett 1975;53:262-6.
    • (1975) FEBS Lett , vol.53 , pp. 262-266
    • Brown, K.A.1    Ratledge, C.2
  • 65
    • 0018610721 scopus 로고
    • Ferrimycobactin reductase activity from Mycobacterium smegmatis
    • McCready KA, Ratledge C. Ferrimycobactin reductase activity from Mycobacterium smegmatis. J Gen Microbiol 1979;113:67-72.
    • (1979) J Gen Microbiol , vol.113 , pp. 67-72
    • McCready, K.A.1    Ratledge, C.2
  • 66
    • 0015146359 scopus 로고
    • Transport of iron by mycobactin in Mycobacterium smegmatis
    • Ratledge C. Transport of iron by mycobactin in Mycobacterium smegmatis. Biochem Biophys Res Commun 1971;45:856-61.
    • (1971) Biochem Biophys Res Commun , vol.45 , pp. 856-861
    • Ratledge, C.1
  • 67
    • 0036230421 scopus 로고    scopus 로고
    • Identification of [2Fe-2S] clusters in microbial ferrochelatase
    • Dailey TA, Dailey HA. Identification of [2Fe-2S] clusters in microbial ferrochelatase. J Bacteriol 2002;184:2460-4.
    • (2002) J Bacteriol , vol.184 , pp. 2460-2464
    • Dailey, T.A.1    Dailey, H.A.2
  • 68
    • 0017810924 scopus 로고
    • Amounts of iron, haem and related compounds in Mycobacterium smegmatis grown in various concentrations of iron
    • McCready KA, Ratledge C. Amounts of iron, haem and related compounds in Mycobacterium smegmatis grown in various concentrations of iron. Biochem Soc Trans 1978;6:421-3.
    • (1978) Biochem Soc Trans , vol.6 , pp. 421-423
    • McCready, K.A.1    Ratledge, C.2
  • 69
    • 0020288432 scopus 로고
    • Iron transport in Mycobacterium smegmatis: The location of mycobactin by electron microscopy
    • Ratledge C, Patel PV, Mundy J. Iron transport in Mycobacterium smegmatis: the location of mycobactin by electron microscopy. J Gen Microbiol 1982;128:1559-65.
    • (1982) J Gen Microbiol , vol.128 , pp. 1559-1565
    • Ratledge, C.1    Patel, P.V.2    Mundy, J.3
  • 70
  • 71
    • 0032211974 scopus 로고    scopus 로고
    • Identification of a Mycobacterium tuberculosis gene cluster encoding the biosynthetic enzymes for the assembly of the virulence-conferring siderophore mycobactin
    • Quadri LEN, Sello J, Keating TA, Weinreb PH, Walsh CT. Identification of a Mycobacterium tuberculosis gene cluster encoding the biosynthetic enzymes for the assembly of the virulence-conferring siderophore mycobactin. Chem Biol 1998;5:631-45.
    • (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
  • 73
    • 0032544193 scopus 로고    scopus 로고
    • The nonribosomal peptide synthetase HMWP2 forms a thiazoline ring during biogenesis of yersiniabactin, an iron chelating virulence factor of Yersinia pestis
    • Gehring AM, Mori I, Perry RD, Walsh CT. The nonribosomal peptide synthetase HMWP2 forms a thiazoline ring during biogenesis of yersiniabactin, an iron chelating virulence factor of Yersinia pestis. Biochemistry 1998;37: 11637-50.
    • (1998) Biochemistry , vol.37 , pp. 11637-11650
    • Gehring, A.M.1    Mori, I.2    Perry, R.D.3    Walsh, C.T.4
  • 74
    • 0015529266 scopus 로고
    • Salicylic acid biosynthesis and its control in Mycobacterium smegmatis
    • Marshall BJ, Ratledge C. Salicylic acid biosynthesis and its control in Mycobacterium smegmatis. Biochim Biophys Acta 1972;264:106-16.
    • (1972) Biochim Biophys Acta , vol.264 , pp. 106-116
    • Marshall, B.J.1    Ratledge, C.2
  • 75
    • 0000055469 scopus 로고
    • Nutrition, growth and metabolism
    • Ratledge C, Stanford J, editors. London: Academic Press
    • Ratledge C. Nutrition, growth and metabolism. In: Ratledge C, Stanford J, editors. The biology of the mycobacteria, vol. 1. London: Academic Press; 1982. p. 85-271.
    • (1982) The Biology of the Mycobacteria , vol.1 , pp. 85-271
    • Ratledge, C.1
  • 76
    • 0032918010 scopus 로고    scopus 로고
    • Identification of Fur, aconitase, and other proteins expressed by Mycobacterium tuberculosis under conditions of low and high concentrations of iron by combined two-dimensional gel electrophoresis and mass spectrometry
    • Wong DK, Lee BY, Horwitz MA, Gibson BW. Identification of Fur, aconitase, and other proteins expressed by Mycobacterium tuberculosis under conditions of low and high concentrations of iron by combined two-dimensional gel electrophoresis and mass spectrometry. Infect Immun 1999;67:327-36.
    • (1999) Infect Immun , vol.67 , pp. 327-336
    • Wong, D.K.1    Lee, B.Y.2    Horwitz, M.A.3    Gibson, B.W.4
  • 78
    • 0002961085 scopus 로고    scopus 로고
    • Gene expression and regulation
    • Ratledge C, Dale J, editors. Oxford, UK: Blackwell Science
    • Timm J, Gomez M, Smith I. Gene expression and regulation. In: Ratledge C, Dale J, editors. Mycobacteria: molecular biology and virulence. Oxford, UK: Blackwell Science; 1999. p. 59-92.
    • (1999) Mycobacteria: Molecular Biology and Virulence , pp. 59-92
    • Timm, J.1    Gomez, M.2    Smith, I.3
  • 79
    • 0035169902 scopus 로고    scopus 로고
    • The Mycobacterium tuberculosis IdeR is a dual functional regulator that controls transcription of glues involved in iron acquisition, iron storage and survival in macrophages
    • Gold B, Rodriguez GM, Marras SAE, Pentecost M, Smith I. The Mycobacterium tuberculosis IdeR is a dual functional regulator that controls transcription of glues involved in iron acquisition, iron storage and survival in macrophages. Mol Microbiol 2001;42:851-65.
    • (2001) Mol Microbiol , vol.42 , pp. 851-865
    • Gold, B.1    Rodriguez, G.M.2    Marras, S.A.E.3    Pentecost, M.4    Smith, I.5
  • 80
    • 0033607166 scopus 로고    scopus 로고
    • Attenuation of virulence in Mycobacterium tuberculosis expressing a constitutively active iron repressor
    • Manabe YC, Saviola BJ, Sun L, Murphy JR, Bishai WR. Attenuation of virulence in Mycobacterium tuberculosis expressing a constitutively active iron repressor. Proc Natl Acad Sci USA 1999;96:12844-8.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 12844-12848
    • Manabe, Y.C.1    Saviola, B.J.2    Sun, L.3    Murphy, J.R.4    Bishai, W.R.5
  • 81
    • 0001779403 scopus 로고
    • True, false chlorosis
    • London: The New Sydenham Society; also published by Lindsay & Blakiston, Philadelphia
    • Trousseau A. True, false chlorosis. In: Lectures on clinical medicine, vol. 5. London: The New Sydenham Society; 1872. p. 95-117 [also published by Lindsay & Blakiston, Philadelphia].
    • (1872) Lectures on Clinical Medicine , vol.5 , pp. 95-117
    • Trousseau, A.1
  • 82
    • 0027402608 scopus 로고
    • The development of awareness of iron-withholding defense
    • Weinberg ED. The development of awareness of iron-withholding defense. Perspect Biol Med 1993;36:215-21.
    • (1993) Perspect Biol Med , vol.36 , pp. 215-221
    • Weinberg, E.D.1
  • 84
    • 0030496566 scopus 로고    scopus 로고
    • Role of mammalian serum on in vitro growth of Mycobacterium avium
    • Dhople AM, Ibanez MA, Poirer TC. Role of mammalian serum on in vitro growth of Mycobacterium avium. Biomed Lett 1996;53:155-61.
    • (1996) Biomed Lett , vol.53 , pp. 155-161
    • Dhople, A.M.1    Ibanez, M.A.2    Poirer, T.C.3
  • 85
    • 0030338523 scopus 로고    scopus 로고
    • Role of Iron in the pathogenesis of Mycobacterium avium infection in mice
    • Dhople AM, Ibanez MA, Poirer TC. Role of Iron in the pathogenesis of Mycobacterium avium infection in mice. Microbios 1996;87:77-87.
    • (1996) Microbios , vol.87 , pp. 77-87
    • Dhople, A.M.1    Ibanez, M.A.2    Poirer, T.C.3
  • 86
    • 0035143276 scopus 로고    scopus 로고
    • Role of iron in experimental Mycobacterium avium infection
    • Gomez MS, Boelaert JR, Appelberg R. Role of iron in experimental Mycobacterium avium infection. J Clin Virol 2001;20:117-22.
    • (2001) J Clin Virol , vol.20 , pp. 117-122
    • Gomez, M.S.1    Boelaert, J.R.2    Appelberg, R.3
  • 88
    • 0002162781 scopus 로고
    • Poro-aminosalicylic acid in the treatment of tuberculosis
    • Lehmann J. Poro-aminosalicylic acid in the treatment of tuberculosis. Lancet 1946;1:15-6.
    • (1946) Lancet , vol.1 , pp. 15-16
    • Lehmann, J.1
  • 89
    • 0016591187 scopus 로고
    • The effect of p-aminosalicylic acid on iron transport and assimilation in mycobacteria
    • Brown KA, Ratledge C. The effect of p-aminosalicylic acid on iron transport and assimilation in mycobacteria. Biochim Biophys Acta 1975;385:207-20.
    • (1975) Biochim Biophys Acta , vol.385 , pp. 207-220
    • Brown, K.A.1    Ratledge, C.2
  • 90
    • 0015434588 scopus 로고
    • Inhibition of mycobactin formation in Mycobacterium smegmatis by p-aminosalicylic acid. A new proposal for the mode of action of PAS
    • Ratledge C, Brown KA. Inhibition of mycobactin formation in Mycobacterium smegmatis by p-aminosalicylic acid. A new proposal for the mode of action of PAS. Am Rev Respir Dis 1972;106:774-6.
    • (1972) Am Rev Respir Dis , vol.106 , pp. 774-776
    • Ratledge, C.1    Brown, K.A.2
  • 91
    • 0015384573 scopus 로고
    • Isolation and properties of auxotrophic mutants of Mycobacterium smegmatis requiring salicylic acid or mycobactin
    • Ratledge C, Hall MJ. Isolation and properties of auxotrophic mutants of Mycobacterium smegmatis requiring salicylic acid or mycobactin. J Gen Microbiol 1972;72: 143-50.
    • (1972) J Gen Microbiol , vol.72 , pp. 143-150
    • Ratledge, C.1    Hall, M.J.2
  • 92
    • 0346574395 scopus 로고
    • Pura-aminosalicylic acid. Part II. The in vitro tuberculostatic behaviour of para-aminosalicylic acid and related compounds
    • Goodacre CL, Mitchell BW, Seymour DE. Pura-aminosalicylic acid. Part II. The in vitro tuberculostatic behaviour of para-aminosalicylic acid and related compounds. Q J Pharm 1948;21:301-5.
    • (1948) Q J Pharm , vol.21 , pp. 301-305
    • Goodacre, C.L.1    Mitchell, B.W.2    Seymour, D.E.3
  • 93
    • 0342587525 scopus 로고
    • The antibacterial action of streptomycin, isoniazid and PAS
    • Barry V, editor. London: Butterworths
    • Winder F. The antibacterial action of streptomycin, isoniazid and PAS. In: Barry V, editor. Chemotherapy of tuberculosis. London: Butterworths; 1964. p. 111-49.
    • (1964) Chemotherapy of Tuberculosis , pp. 111-149
    • Winder, F.1
  • 94
    • 0014836881 scopus 로고
    • Early steps in the biosynthesis of mycobactins P and S
    • Tateson JE. Early steps in the biosynthesis of mycobactins P and S. Biochem J 1970;118:747-53.
    • (1970) Biochem J , vol.118 , pp. 747-753
    • Tateson, J.E.1
  • 95
    • 0036148173 scopus 로고    scopus 로고
    • Effects on Mycobacterium avium replication in normal human macrophages by deferiprone (L1) and other iron chelators
    • Douvas GS, May MH, Kolnagou A, Koutoghiorghes GJ. Effects on Mycobacterium avium replication in normal human macrophages by deferiprone (L1) and other iron chelators. Arzneim-Forsch Drug Res 2002;52:45-52.
    • (2002) Arzneim-Forsch Drug Res , vol.52 , pp. 45-52
    • Douvas, G.S.1    May, M.H.2    Kolnagou, A.3    Koutoghiorghes, G.J.4
  • 96
    • 0030855151 scopus 로고    scopus 로고
    • Evaluation of growth promotion and inhibition from mycobactin and non-mycobacterial siderophores (desferrioxasmine and FR160) in Mycobacterium aurum
    • Bosne-David S, Bricard L, Ramiandrasoa F, DeRoussent A, Kunesch A, Andrewmont A. Evaluation of growth promotion and inhibition from mycobactin and non-mycobacterial siderophores (desferrioxasmine and FR160) in Mycobacterium aurum. Antimicrob Agents Chemother 1997;41: 1837-9.
    • (1997) Antimicrob Agents Chemother , vol.41 , pp. 1837-1839
    • Bosne-David, S.1    Bricard, L.2    Ramiandrasoa, F.3    DeRoussent, A.4    Kunesch, A.5    Andrewmont, A.6
  • 97
    • 0007464054 scopus 로고    scopus 로고
    • Siderophore transport in mycobacteria analysed by Mössbauer spectroscopy possible routes to novel antibiotics against these organisms?
    • Matzanke BF, Möllmann U, Reissbrodt R, Schünemann V, Trautwein AX. Siderophore transport in mycobacteria analysed by Mössbauer spectroscopy possible routes to novel antibiotics against these organisms? Hyperfine Interactions 1998;112:123-8.
    • (1998) Hyperfine Interactions , vol.112 , pp. 123-128
    • Matzanke, B.F.1    Möllmann, U.2    Reissbrodt, R.3    Schünemann, V.4    Trautwein, A.X.5
  • 98
    • 0034812578 scopus 로고    scopus 로고
    • Inhibition of the in-vitro growth of Mycobacterium tuberculosis by a phytosiderophore
    • Rajir J, Dam T, Kumar S, Bose M, Aggarwal KK, Babu CR. Inhibition of the in-vitro growth of Mycobacterium tuberculosis by a phytosiderophore. J Med Microbiol 2001;50:916-8.
    • (2001) J Med Microbiol , vol.50 , pp. 916-918
    • Rajir, J.1    Dam, T.2    Kumar, S.3    Bose, M.4    Aggarwal, K.K.5    Babu, C.R.6
  • 99
    • 0035032561 scopus 로고    scopus 로고
    • Screening system for xenosiderophores as potential drugs/delivery agents in mycobacteria
    • Schumann G, Mollmann U. Screening system for xenosiderophores as potential drugs/delivery agents in mycobacteria. Antimicrob Agents Chemother 2001;45: 1317-22.
    • (2001) Antimicrob Agents Chemother , vol.45 , pp. 1317-1322
    • Schumann, G.1    Mollmann, U.2
  • 100
    • 0030975106 scopus 로고    scopus 로고
    • Total synthesis of a mycobactin S, a siderophore and growth promoter of Mycobacterium smegmatis, and determination of its growth inhibitory activity against Mycobacterium tuberculosis
    • Hu J, Miller MJ. Total synthesis of a mycobactin S, a siderophore and growth promoter of Mycobacterium smegmatis, and determination of its growth inhibitory activity against Mycobacterium tuberculosis. J Am Chem Soc 1997;119:3462-8.
    • (1997) J Am Chem Soc , vol.119 , pp. 3462-3468
    • Hu, J.1    Miller, M.J.2
  • 101
    • 0032569011 scopus 로고    scopus 로고
    • Total synthesis of mycobactin analogues as potent antimycobacterial agents using a minimal protecting group strategy
    • Xu Y, Miller JJ. Total synthesis of mycobactin analogues as potent antimycobacterial agents using a minimal protecting group strategy. J Org Chem 1998;63:431-522.
    • (1998) J Org Chem , vol.63 , pp. 431-522
    • Xu, Y.1    Miller, J.J.2
  • 102
    • 0022976179 scopus 로고
    • Metal analogues of mycobacterin and exochelin fail to act as effective antimycobacterial agents
    • Barclay R, Ratledge C. Metal analogues of mycobacterin and exochelin fail to act as effective antimycobacterial agents. Z Bakt Mikrobiol Hyg 1986;A264:203-7.
    • (1986) Z Bakt Mikrobiol Hyg , vol.A264 , pp. 203-207
    • Barclay, R.1    Ratledge, C.2
  • 103
    • 0032937984 scopus 로고    scopus 로고
    • Non-iron metalloporphyrins: Potent antibacterial compounds that exploit haem/Hb uptake systems of pathogenic bacteria
    • Stojiljkovic I, Kumar V, Srinivasan N. Non-iron metalloporphyrins: potent antibacterial compounds that exploit haem/Hb uptake systems of pathogenic bacteria. Mol Microbiol 1999;31:429-42.
    • (1999) Mol Microbiol , vol.31 , pp. 429-442
    • Stojiljkovic, I.1    Kumar, V.2    Srinivasan, N.3
  • 107
    • 0025836059 scopus 로고
    • Uptake of a catecholic cephalosporin by the iron transport system of Escherichia coli
    • Critchley IA, Basker MJ, Edmondson RA, Knott SJ. Uptake of a catecholic cephalosporin by the iron transport system of Escherichia coli. J Antimicrob Chemother 1991;28:377-88.
    • (1991) J Antimicrob Chemother , vol.28 , pp. 377-388
    • Critchley, I.A.1    Basker, M.J.2    Edmondson, R.A.3    Knott, S.J.4
  • 108
    • 0033986977 scopus 로고    scopus 로고
    • Use of genomics and combinational chemistry in the development of new antimycobacterial drugs
    • Barry III CE, Slayden RA, Sampson AE, Lee RE. Use of genomics and combinational chemistry in the development of new antimycobacterial drugs. Biochem Pharmacol 2000;59:221-31.
    • (2000) Biochem Pharmacol , vol.59 , pp. 221-231
    • Barry III, C.E.1    Slayden, R.A.2    Sampson, A.E.3    Lee, R.E.4
  • 109
    • 33846640634 scopus 로고    scopus 로고
    • Antibiotics and antibiotic resistance in mycobacteria
    • Ratledge C, Dale JW, editors. Oxford, UK: Blackwell Science
    • Webb V, Davies J. Antibiotics and antibiotic resistance in mycobacteria. In: Ratledge C, Dale JW, editors. Mycobacteria virulence and molecular biology. Oxford, UK: Blackwell Science; 1999. p. 287-306.
    • (1999) Mycobacteria Virulence and Molecular Biology , pp. 287-306
    • Webb, V.1    Davies, J.2


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