메뉴 건너뛰기




Volumn 18, Issue 11, 2011, Pages 1723-1731

Iron regulation in tuberculosis research: Promise and challenges

Author keywords

Drug targets; Iron modulation; Iron regulation; Iron sulfur cluster proteins; Tuberculosis

Indexed keywords

3 NITROPROPIONIC ACID; AMINOSALICYLIC ACID; ENZYME INHIBITOR; IRON; IRON SULFUR PROTEIN; TRIAZOLE DERIVATIVE;

EID: 79955700930     PISSN: 09298673     EISSN: None     Source Type: Journal    
DOI: 10.2174/092986711795471301     Document Type: Article
Times cited : (16)

References (127)
  • 2
    • 0033986292 scopus 로고    scopus 로고
    • Mutational analysis of a role for salicylic acid in iron metabolism of Mycobacterium smegmatis
    • DOI 10.1128/JB.182.2.264-271.2000
    • Adilakshmi, T.; Ayling, P. D.; Ratledge, C. Mutational analysis of a role for salicylic acid in iron metabolism of Mycobacterium smegmatis. J. Bacteriol. 2000, 182, 264-271. (Pubitemid 30030107)
    • (2000) Journal of Bacteriology , vol.182 , Issue.2 , pp. 264-271
    • Adilakshmi, T.1    Ayling, P.D.2    Ratledge, C.3
  • 3
    • 33846942978 scopus 로고    scopus 로고
    • Molecular function of whiB4/Rv3681C of Mycobacterium tuberculosis H37Rv, a [4Fe-4S] cluster co-ordinating protein disulphide reductase
    • Alam, M. S.; Garg, S. K.; Agarwal, P. Molecular function of whiB4/Rv3681C of Mycobacterium tuberculosis H37Rv, a [4Fe-4S] cluster co-ordinating protein disulphide reductase. Mol. Microbiol., 2007, 63, 1414-1431.
    • (2007) Mol. Microbiol , vol.63 , pp. 1414-1431
    • Alam, M.S.1    Garg, S.K.2    Agarwal, P.3
  • 4
    • 47749094628 scopus 로고    scopus 로고
    • Matrix assisted refolding and redox properties of WhiB3/Rv3416 of Mycobacterium tuberculosis H37Rv
    • Alam, M. S.; Agrawal, P. Matrix assisted refolding and redox properties of WhiB3/Rv3416 of Mycobacterium tuberculosis H37Rv. Prot. Expr. Purif., 2008, 61, 83-91.
    • (2008) Prot. Expr. Purif , vol.61 , pp. 83-91
    • Alam, M.S.1    Agrawal, P.2
  • 5
    • 0037132556 scopus 로고    scopus 로고
    • LytB protein catalyzes the terminal step of the 2-C-methyl-D-erythritol- 4-phosphate pathway of isoprenoid biosynthesis
    • DOI 10.1016/S0014-5793(02)03726-2, PII S0014579302037262
    • Altanicicek, B.; Duin, E. C.; Reichenberg, A.; Hedderich, R.; Kollas, A. K.; Hinz, M.; Wagner, S.; Wiesner J.; Beck, E.; Joma, H. LytB protein catalyzes the terminal step of the 2-C-methyl-D-eryhthritol-4-phosphate pathway of isoprenoid biosynthesis. FEBS Lett., 2002, 532, 437-440. (Pubitemid 35441389)
    • (2002) FEBS Letters , vol.532 , Issue.3 , pp. 437-440
    • Altincicek, B.1    Duin, E.C.2    Reichenberg, A.3    Hedderich, R.4    Kollas, A.-K.5    Hintz, M.6    Wagner, S.7    Wiesner, J.8    Beck, E.9    Jomaa, H.10
  • 6
    • 0028290569 scopus 로고
    • Effective vaccination of mice against Mycobacterium tuberculosis infection with a soluble mixture of secreted mycobacterial proteins
    • Andersen, P. Effective vaccination of mice against Mycobacterium tuberculosis infection with a soluble mixture of secreted mycobacterial proteins. Infect. Immunol., 1994, 62, 2536-2544. (Pubitemid 24157087)
    • (1994) Infection and Immunity , vol.62 , Issue.6 , pp. 2536-2544
    • Andersen, P.1
  • 8
    • 77953161443 scopus 로고    scopus 로고
    • Respiratory ATP synthesis: The new generation of mycobacterial drug targets?
    • Bald, D.; Koul, A. Respiratory ATP synthesis: the new generation of mycobacterial drug targets? FEMS Microbiol. Lett., 2010, 1-7.
    • (2010) FEMS Microbiol. Lett , pp. 1-7
    • Bald, D.1    Koul, A.2
  • 9
    • 0000989147 scopus 로고    scopus 로고
    • Aconitase as iron-sulfur protein, enzyme and iron-regulatory protein
    • Beinert, H.; Kennedy, M. C.; Stout, C. D. Aconitase as iron-sulfur protein, enzyme and iron-regulatory protein. Chem. Rev., 1996, 96, 2335-2374.
    • (1996) Chem. Rev , vol.96 , pp. 2335-2374
    • Beinert, H.1    Kennedy, M.C.2    Stout, C.D.3
  • 10
    • 0034003112 scopus 로고    scopus 로고
    • Iron-sulfur proteins: Ancient structures, still full of surprises
    • Beinert, H. Iron-sulfur proteins, ancient structures, still full of surprises. J. Biol. Inorg. Chem., 2000, 5, 2-15. (Pubitemid 30120582)
    • (2000) Journal of Biological Inorganic Chemistry , vol.5 , Issue.1 , pp. 2-15
    • Beinert, H.1
  • 11
    • 0031767535 scopus 로고    scopus 로고
    • A Mycobacterium tuberculosis operon encoding ESAT-6 and a novel low-molecular-mass culture filtrate protein (CFP-10)
    • Berthet, F. X.; Rasmussen, P. B.; Rosenkrands, I.; Andersen, P.; Gicquel, B. A. Mycobacterium tuberculosis operon encoding ESAT-6 and a novel lowmolecular- mass culture filtrate protein (CFP-10). Microbiology, 1998, 144, 3195-203. (Pubitemid 28515598)
    • (1998) Microbiology , vol.144 , Issue.11 , pp. 3195-3203
    • Berthet, F.-X.1    Rasmussen, P.B.2    Rosenkrands, I.3    Andersen, P.4    Gicquel, B.5
  • 12
    • 33751296525 scopus 로고    scopus 로고
    • Human milk glycoproteins inhibit the adherence of salmonella typhimurium to HeLa cells
    • Besseler, H. C.; de Oliveira, I. R.; Giugliano, L. G. Human milk glycoroteins inhibit the adherence of salonella typhimurium to HeLa cells. Microbiol. Immunol., 2006, 50, 877-882. (Pubitemid 44800380)
    • (2006) Microbiology and Immunology , vol.50 , Issue.11 , pp. 877-882
    • Bessler, H.C.1    De Oliveira, I.R.2    Giugliano, L.G.3
  • 14
    • 0028905679 scopus 로고
    • Human T-cell responses to secreted antigen fractions of Mycobacterium tuberculosis
    • Boesen, H.; Jensen, B. N.; Wilcke, T.; Andersen, P. Human T-cell responses to secreted antigen fractions of Mycobacterium tuberculosis. Infect. Immunol., 1995, 6 , 1491-1497.
    • (1995) Infect. Immunol , vol.6 , pp. 1491-1497
    • Boesen, H.1    Jensen, B.N.2    Wilcke, T.3    Andersen, P.4
  • 15
    • 0034307852 scopus 로고    scopus 로고
    • The iron dependent regulatory protein IdeR DtxR of Rhodococcus equi
    • Boland, C. A.; Meijer, W. G. The iron dependent regulatory protein IdeR DtxR of Rhodococcus equi. FEMS Microbiol. Lett., 2000, 191, 1-5.
    • (2000) FEMS Microbiol. Lett , vol.191 , pp. 1-5
    • Boland, C.A.1    Meijer, W.G.2
  • 16
    • 0030855151 scopus 로고    scopus 로고
    • Evaluation of growth promotion and inhibition from mycobactins and nonmycobacterial siderophores (Desferrioxamine and FR160) in Mycobacterium aurum
    • Bosne, D. S.; Bricard, L.; Ramiandrasoa, F.; DeRoussent, A.; Kunesch, A.; Andrewmont, A. Evaluation of growth and inhibition from mycobactin and non-mycobacterial siderophores (desferrioxamine and FR160) in Mycobacterium aurum. Antimicrob. Agents Chemother., 1997, 41, 1837-1839. (Pubitemid 27339901)
    • (1997) Antimicrobial Agents and Chemotherapy , vol.41 , Issue.8 , pp. 1837-1839
    • Bosne-David, S.1    Bricard, L.2    Ramiandrasoa, F.3    DeRoussent, A.4    Kunesch, G.5    Andremont, A.6
  • 17
    • 0034064468 scopus 로고    scopus 로고
    • A parallel intraphagosomal survival strategy shared by Mycobacterium tuberculosis and Salmonella enterica
    • DOI 10.1046/j.1365-2958.2000.01797.x
    • Buchmeier, N., Blanc-Potard, A., Ehrt, S., Piddington, D., Riley, L., Groisman, E. A. A parallel intraphagosomal survival strategy shared by Mycobacterium tuberculosis and Salmonella enterica. Mol. Microbiol., 2000, 35, 1375-82. (Pubitemid 30175513)
    • (2000) Molecular Microbiology , vol.35 , Issue.6 , pp. 1375-1382
    • Buchmeier, N.1    Blanc-Potard, A.2    Ehrt, S.3    Piddington, D.4    Riley, L.5    Groisman, E.A.6
  • 18
    • 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
    • DOI 10.1006/mpat.1997.9999
    • Calder, K. M.; Horwitz, M. A. Identification of iron-regulated proteins of Mycobacterium tuberculosis and cloning of tandem genes encoding low iron induced protein and a metal transporting ATPase with similarities to twocomponent metal transport system. Microb. Pathog. 1998, 24, 133-143. (Pubitemid 28138571)
    • (1998) Microbial Pathogenesis , vol.24 , Issue.3 , pp. 133-143
    • Calder, K.M.1    Horwitz, M.A.2
  • 19
    • 67649586805 scopus 로고    scopus 로고
    • Structural insight into the heme-based redox sensing by DosS from Mycobacterium tuberculosis
    • Cho, H. Y., Cho, H. J., Kim, Y. M., Oh, J. I., Kang, B. S. Structural insight into the heme-based redox sensing by DosS from Mycobacterium tuberculosis. J. Biol. Chem., 2009, 284, 13057-67.
    • (2009) J. Biol. Chem , vol.284 , pp. 13057-67
    • Cho, H.Y.1    Cho, H.J.2    Kim, Y.M.3    Oh, J.I.4    Kang, B.S.5
  • 20
    • 0029905151 scopus 로고    scopus 로고
    • The Mycobacterium tuberculosis phagosome interacts with early endosomes and is accessible to exogenously administered transferrin
    • DOI 10.1084/jem.184.4.1349
    • Clemens, D. L.; Horwitz, M. A. The Mycobacterium tuberculosis phagosome interacts with early endosomes and is accessible to exogenously administered transferrin. J. Exp. Med., 1996, 184, 1349-1355. (Pubitemid 26354691)
    • (1996) Journal of Experimental Medicine , vol.184 , Issue.4 , pp. 1349-1355
    • Clemens, D.L.1    Horwitz, M.A.2
  • 21
    • 0033400131 scopus 로고    scopus 로고
    • Prospects for the development of new vaccine adjuvants
    • Cox, J.; Coulter, A. Prospects for the development of new vaccine adjuvants. BioDrugs, 1999, 12, 439-53. (Pubitemid 30017215)
    • (1999) BioDrugs , vol.12 , Issue.6 , pp. 439-453
    • Cox, J.1    Coulter, A.2
  • 22
    • 0035989334 scopus 로고    scopus 로고
    • Immuno-informatics: Mining genomes for vaccine components
    • DOI 10.1046/j.1440-1711.2002.01092.x
    • De Groot, A. S.; Sbai, H.; Aubin, C. S.; McMurry, J.; Martin, W. Immunoinformatics, Mining genomes for vaccine development. Immunol. Cell Biol. 2002, 80, 255-269. (Pubitemid 34639376)
    • (2002) Immunology and Cell Biology , vol.80 , Issue.3 , pp. 255-269
    • De Groot, A.S.1    Sbai, H.2    Aubin, C.S.3    McMurry, J.4    Martin, W.5
  • 23
    • 0032734070 scopus 로고    scopus 로고
    • T-cell recognition of Mycobacterium tuberculosis culture filtrate fractions in tuberculosis patients and their household contacts
    • Demissie, A.; Ravn, P.; Olobo, J.; Dohorty, T. M.; Eguale, T.; Geletu, M.; Helu W.; Andersen, P.; Britton, S. T-cell recognition of Mycobacterium tuberculosis culture filtrate fractions in tuberculosis patients and their household contacts. Infect. Immunol. , 1999, 67, 5967-5971. (Pubitemid 29508125)
    • (1999) Infection and Immunity , vol.67 , Issue.11 , pp. 5967-5971
    • Demissie, A.1    Ravn, P.2    Olobo, J.3    Doherty, T.M.4    Eguale, T.5    Geletu, M.6    Hailu, W.7    Andersen, P.8    Britton, S.9
  • 24
    • 0035724513 scopus 로고    scopus 로고
    • The Fur repressor controls transcription of iron-activated and -repressed genes in Helicobacter pylori
    • DOI 10.1046/j.1365-2958.2001.02696.x
    • Delany, I.; Spohn, G.; Rappuoli, R.; Scarlato, V. The fur repressor controls transcription of iron-activated and -repressed genes in Helicobacter pylori. Mol. Microbiol., 2001, 42, 1297-1309. (Pubitemid 34209090)
    • (2001) Molecular Microbiology , vol.42 , Issue.5 , pp. 1297-1309
    • Delany, I.1    Spohn, G.2    Rappuoli, R.3    Scarlato, V.4
  • 25
    • 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. Operator sequences of the aerobactin operon of plasmid ColV-K30 binding the ferric uptake regulation (fur) repressor. J. Bacteriol. 1987, 169, 2624-2630. (Pubitemid 17104324)
    • (1987) Journal of Bacteriology , vol.169 , Issue.6 , pp. 2624-2630
    • De Lorenzo, V.1    Wee, S.2    Herrero, M.3    Neilands, J.B.4
  • 29
    • 0030338523 scopus 로고    scopus 로고
    • Role of iron in the pathogenesis of Mycobacterium avium infection in mice
    • Dhopl, A. M.; Ibanez, M. A.; Poirier, T. C. Role of iron in the pathogenesis of Mycobacterium avium infection in mice. Microbios, 1996, 87, 77-87. (Pubitemid 126528878)
    • (1996) Microbios , vol.87 , Issue.351 , pp. 77-87
    • Dhople, A.M.1    Ibanez, M.A.2    Poirier, T.C.3
  • 30
    • 19744376797 scopus 로고    scopus 로고
    • Contribution of the Mycobacterium tuberculosis MmpL protein family to virulence and drug resistance
    • DOI 10.1128/IAI.73.6.3492-3501.2005
    • Domenech, P.; Reed, M. B.; Berry C. E. 3rd contribution of Mycobacterium tuberculosis MmpL protein family to virulence and drug resistance. Infect Immun., 2005, 73, 3492-3501. (Pubitemid 40745893)
    • (2005) Infection and Immunity , vol.73 , Issue.6 , pp. 3492-3501
    • Domenech, P.1    Reed, M.B.2    Barry III, C.E.3
  • 31
    • 70450282398 scopus 로고    scopus 로고
    • Rapid and spontaneous loss of Phthiocerol Dimycocerosate (PDIM) from Mycobacterium tuberculosis grown in-vitro, implications for virulence studies
    • Domenech, P.; Reed, M. B. Rapid and spontaneous loss of Phthiocerol Dimycocerosate (PDIM) from Mycobacterium tuberculosis grown in-vitro, implications for virulence studies. Microbiology, 2009, 155, 3532-3543.
    • (2009) Microbiology , vol.155 , pp. 3532-3543
    • Domenech, P.1    Reed, M.B.2
  • 33
    • 0034073375 scopus 로고    scopus 로고
    • Oxygenated mycolic acids are necessary for virulence of Mycobacterium tuberculosis in mice
    • DOI 10.1046/j.1365-2958.2000.01882.x
    • Dubnau, E.; Chan, J.; Raynaud, C.; Mohan, V. P.; Lanéelle, M. A.; Yu, K.; Quémard, A.; Smith, I.; Daffé, M. Oxygenated mycolic acids are necessary for virulence of Mycobacterium tuberculosis in mice. Mol. Microbiol., 2000, 36, 630-637. (Pubitemid 30258847)
    • (2000) Molecular Microbiology , vol.36 , Issue.3 , pp. 630-637
    • Dubnau, E.1    Chan, J.2    Raynaud, C.3    Mohan, V.P.4    Laneelle, M.-A.5    Yu, K.6    Quemard, A.7    Smith, I.8    Daffe, M.9
  • 34
    • 0029809920 scopus 로고    scopus 로고
    • An ideR mutant of Mycobacterium smegmatis has derepressed siderophore production and an altered oxidative-stress response
    • Dussurget, O.; Rodriguez, M.; Smith, I. An IdeR mutant of Mycobacterium smegmatis has a derepressed siderophore production and an altered oxidative stress response. Mol Microbiol., 1996, 22, 535-544. (Pubitemid 26373837)
    • (1996) Molecular Microbiology , vol.22 , Issue.3 , pp. 535-544
    • Dussurget, O.1    Rodriguez, M.2    Smith, I.3
  • 35
    • 0032167951 scopus 로고    scopus 로고
    • Interdependence of mycobacterial iron regulation, oxidative-stress response and isoniazid resistance
    • DOI 10.1016/S0966-842X(98)01307-9, PII S0966842X98013079
    • Dussurget, O.; Smith, I. Interdependence of mycobacterial iron regulation, oxidative stress response and isoniazid resistance. Trends Microbiol., 1998, 6, 354-358. (Pubitemid 28473195)
    • (1998) Trends in Microbiology , vol.6 , Issue.9 , pp. 354-358
    • Dussurget, O.1    Smith, I.2
  • 36
    • 33644991496 scopus 로고    scopus 로고
    • Global epidemiology of tuberculosis
    • Dye, C. Global epidemiology of tuberculosis. Lancet, 2006, 367, 938-940.
    • (2006) Lancet , vol.367 , pp. 938-940
    • Dye, C.1
  • 37
    • 70449513046 scopus 로고    scopus 로고
    • A systems biology framework for modeling metabolic enzyme inhibition of Mycobacterium tuberculosis BMC Syst
    • Fang, X.; Wallqvist, A.; Reifman, J. A systems biology framework for modeling metabolic enzyme inhibition of Mycobacterium tuberculosis BMC Syst. Biol. 2009, 3, 92.
    • (2009) Biol , vol.3 , pp. 92
    • Fang, X.1    Wallqvist, A.2    Reifman, J.3
  • 38
    • 0037224238 scopus 로고    scopus 로고
    • Activities of moxifloxacin alone and in combination with other antimicrobial agents against multidrug-resistant Mycobacterium tuberculosis infection in BALB/c mice
    • DOI 10.1128/AAC.47.1.360-362.2003
    • Fattorini, L.; Tan, D.; Iona, E, ; Mattei, M.; Giannoni, F.; Brunori, L.; Recchia, S.; Orefici, G. Activities of moxifloxacin alone and in combination with other antimicrobial agents against multi-drug resistant Mycobacterium tuberculosis infection in BALB/c mice. Antimicrob. Agents Chemoth., 2003, 47, 360-362. (Pubitemid 36070385)
    • (2003) Antimicrobial Agents and Chemotherapy , vol.47 , Issue.1 , pp. 360-362
    • Fattorini, L.1    Tan, D.2    Iona, E.3    Mattei, M.4    Giannoni, F.5    Brunori, L.6    Recchia, S.7    Orefici, G.8
  • 39
    • 33344469904 scopus 로고    scopus 로고
    • Smallmolecule 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. Smallmolecule inhibition of siderophore biosynthesis in Mycobacterium tuberculosis and Yersinia pestis. Nat. Chem. Biol., 2005, 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.5
  • 40
    • 0028872014 scopus 로고
    • Variation in protection by BCG Implications of and for heterologous immunity
    • Fine, P. E. Variation in protection by BCG, Implications of and for heterologous immunity. Lancet, 1995, 346, 1339-1345.
    • (1995) Lancet , vol.346 , pp. 1339-1345
    • Fine, P.E.1
  • 41
    • 0028127357 scopus 로고
    • Identification of genes involved in the sequestration of iron in mycobacteria: The ferric exochelin biosynthetic and uptake pathways
    • DOI 10.1111/j.1365-2958.1994.tb02189.x
    • Fiss, E. H.; Yu, S.; Jacobs, W. R. Jr. Identification of genes involved in the sequestration of iron in mycobacteria, the ferric exochelin biosynthetic and uptake pathways. Mol. Microbiol., 1994, 14, 557-569. (Pubitemid 24337335)
    • (1994) Molecular Microbiology , vol.14 , Issue.3 , pp. 557-569
    • Fiss, E.H.1    Yu, S.2    Jacobs Jr., W.R.3
  • 42
    • 0037397764 scopus 로고    scopus 로고
    • Formation of iron-sulfur clusters in bacteria: An emerging field in bioinorganic chemistry
    • DOI 10.1016/S1367-5931(03)00021-8
    • Frazzon, J.; Dean, D.R. Formation of iron-sulfur clusters in bacteria-an emerging field in bioorganic chemistry. Curr. Opin. Chem. Biol., 2003, 7, 166-173. (Pubitemid 36514947)
    • (2003) Current Opinion in Chemical Biology , vol.7 , Issue.2 , pp. 166-173
    • Frazzon, J.1    Dean, D.R.2
  • 43
    • 33748102856 scopus 로고    scopus 로고
    • Hepcidin - A peptide hormone at the interface of innate immunity and iron metabolism
    • Antimicrobial Peptides and Human Disease
    • Ganz, T. Hepcidin a peptide hormone at the interface of innate immunity and iron metabolism. Curr. Top Microbiol. Immunol., 2006, 306, 183-198. (Pubitemid 47400322)
    • (2006) Current Topics in Microbiology and Immunology , vol.306 , pp. 183-198
    • Ganz, T.1
  • 44
    • 0035910583 scopus 로고    scopus 로고
    • The Mycobacterium tuberculosis cmaA2 gene encodes a mycolic acid trans-cyclopropane synthetase
    • DOI 10.1074/jbc.C000652200
    • Glickman, M. S.; Cahill, S. M.; Jacobs, W. R. Jr. The Mycobacterium tuberculosis cmaA2 gene encodes a mycolic acid trans-cyclopropane synthetase. J. Biol. Chem., 2001, 276, 2228-33. (Pubitemid 32109706)
    • (2001) Journal of Biological Chemistry , vol.276 , Issue.3 , pp. 2228-2233
    • Glickman, M.S.1    Cahill, S.M.2    Jacobs Jr., W.R.3
  • 45
    • 0029913805 scopus 로고    scopus 로고
    • Exochelins of Mycobacterium tuberculosis remove iron from human iron binding proteins and donate iron to mycobactins in the M. tuberculosis cell wall
    • Gobin, J.; Horwitz, M. Exochelins of Mycobacterium tuberculosis remove iron from human iron binding proteins and donate iron to mycobactins in the M. tuberculosis cell wall. J. Exp. Med., 1996, 183, 1527-1532.
    • (1996) J. Exp. Med , vol.183 , pp. 1527-1532
    • Gobin, J.1    Horwitz, M.2
  • 46
    • 0034059725 scopus 로고    scopus 로고
    • Identification of secreted proteins of Mycobacterium tuberculosis by a bioinformatic approach
    • DOI 10.1128/IAI.68.4.2323-2327.2000
    • Gomez, M.; Johnson, S.; Gennaro, M. L. Identification of Mycobacterium tuberculosis secreted proteins by a bioinformatic approach. Infect. Immunol., 2000, 68, 2323-2327. (Pubitemid 30164870)
    • (2000) Infection and Immunity , vol.68 , Issue.4 , pp. 2323-2327
    • Gomez, M.1    Johnson, S.2    Gennaro, M.L.3
  • 47
    • 53649106524 scopus 로고    scopus 로고
    • Increased susceptibility to Mycobacterium avium in hemochromatosis protein HFE-deficient mice
    • Gomez-Pereira, S.; Rodriguez, Pedro Nuno, Appelberg, R.; Gomes, M. S. Increased susceptibility to Mycobacterium avium in hemochromatosis protein HFE-deficient mice. Infect. Immun., 2008, 76, 4713-4719.
    • (2008) Infect. Immun , vol.76 , pp. 4713-4719
    • Gomez-Pereira, S.1    Pedro Nuno, R.2    Appelberg, R.3    Gomes, M.S.4
  • 48
    • 0035169902 scopus 로고    scopus 로고
    • The Mycobacterium tuberculosis ideR is a dual functional regulator that controls transcription of genes involved in iron acquisition, iron storage and survival in macrophages
    • DOI 10.1046/j.1365-2958.2001.02684.x
    • Gold. B.; Rodriguez, G.M.; Marras, S.A.; Pentecost, M.; Smith, I. The Mycobacterium tuberculosis IdeR is a dual functional regulator that controls transcription of genes involved in iron acquisition, iron storage and survival in macrophages. Mol. Microbiol., 2001, 42, 851-865. (Pubitemid 33064491)
    • (2001) Molecular Microbiology , vol.42 , Issue.3 , pp. 851-865
    • Gold, B.1    Marcela Rodriguez, G.2    Marras, S.A.E.3    Pentecost, M.4    Smith, I.5
  • 49
    • 9444239308 scopus 로고    scopus 로고
    • Bacterial redox sensors
    • DOI 10.1038/nrmicro1022
    • Green, J.; Paget, M. S. Bacterial redox sensors. Nat. Rev. Microbiol. 2004, 2, 954-966. (Pubitemid 39562534)
    • (2004) Nature Reviews Microbiology , vol.2 , Issue.12 , pp. 954-966
    • Green, J.1    Paget, M.S.2
  • 50
    • 0028113546 scopus 로고
    • Two genetically distinct and differentially regulated aconitases. (AcnA and AcnB) in Escherichia coli
    • Gruer, M. J.; Guest, J. R. Two genetically distinct and differentially regulated aconitases. (AcnA and AcnB) in Escherichia coli. Microbiology, 1994, 140, 2531-2541.
    • (1994) Microbiology , vol.140 , pp. 2531-2541
    • Gruer, M.J.1    Guest, J.R.2
  • 51
    • 57349154252 scopus 로고    scopus 로고
    • Inhibition of Siderophore Biosynthesis by 2-Triazole Substituted Analogues of 5--O-[N-(Salicyl) sulfamoyl] adenosine: Antibacterial Nucleosides Effective against Mycobacterium tuberculosis
    • Gupte, A.; Boshoff, H. I.; Wilson, D. J.; Neres, J.; Labell, N. P.; Somu, R. V.; Xing, C.; Barry III, C. E.; Aldrich, C. C. Inhibition of Siderophore Biosynthesis by 2-Triazole Substituted Analogues of 5--O-[N-(Salicyl) sulfamoyl] adenosine: Antibacterial Nucleosides Effective against Mycobacterium tuberculosis. J. Med. Chem., 2008, 51, 4495-4504.
    • (2008) J. Med. Chem , vol.51 , pp. 4495-4504
    • Gupte, A.1    Boshoff, H.I.2    Wilson, D.J.3    Neres, J.4    Labell, N.P.5    Somu, R.V.6    Xing, C.7    Iii, B.8    E, C.9    Aldrich, C.C.10
  • 52
    • 0035069457 scopus 로고    scopus 로고
    • Iron and metal regulation in bacteria
    • DOI 10.1016/S1369-5274(00)00184-3
    • Hantke, K. Iron and metal regulation in bacteria. Curr. Opin. Microbiol., 2001, 4, 172-177. (Pubitemid 32294419)
    • (2001) Current Opinion in Microbiology , vol.4 , Issue.2 , pp. 172-177
    • Hantke, K.1
  • 53
    • 0036263753 scopus 로고    scopus 로고
    • Use of an arrayed promoter-probe library for the identification of macrophage-regulated genes in Mycobacterium tuberculosis
    • Hobson, R. J.; McBride, A. J.; Kempsell, K. E.; Dale, J. W. Use of an arrayed promoter-probe library for the identification of macrophage regulated genes in Mycobacterium tuberculosis. Microbiology, 2002, 148, 1571-1579. (Pubitemid 34567235)
    • (2002) Microbiology , vol.148 , Issue.5 , pp. 1571-1579
    • Hobson, R.J.1    McBride, A.J.A.2    Kempsell, K.E.3    Dale, J.W.4
  • 54
    • 0034114442 scopus 로고    scopus 로고
    • Attenuation of and protection induced by a leucine auxotroph of Mycobacterium tuberculosis
    • DOI 10.1128/IAI.68.5.2888-2898.2000
    • Hondalus, M. K.; Bardarov, S.; Russell, R.; Chan, J.; Jacobs, W. R. Jr.; Bloom, B. R. Attenuation of and protection induced by a leucine auxotroph of Mycobacterium tuberculosis. Infect. Immun. 2000, 68, 2888-98. (Pubitemid 30253869)
    • (2000) Infection and Immunity , vol.68 , Issue.5 , pp. 2888-2898
    • Hondalus, M.K.1    Bardarov, S.2    Russell, R.3    Chan, J.4    Jacobs Jr., W.R.5    Bloom, B.R.6
  • 55
    • 0028950982 scopus 로고
    • Protective immunity against tuberculosis induced by vaccination with major extracellular proteins of Mycobacterium tuberculosis
    • Horwitz, M. A.; Lee, B. W.; Dillon, B. J.; Harth, G. Protective immunity against tuberculosis induced by vaccination with major extracellular proteins of Mycobacterium tuberculosis. Proc. Natl. Acad. Sci. USA, 1995, 92, 1530-1534.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 1530-1534
    • Horwitz, M.A.1    Lee, B.W.2    Dillon, B.J.3    Harth, G.4
  • 56
    • 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
    • DOI 10.1021/ja963968x, PII S0002786396039686
    • Hu, J.; Miller, M. J. Total synthesis of 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, 3462-3468. (Pubitemid 27226044)
    • (1997) Journal of the American Chemical Society , vol.119 , Issue.15 , pp. 3462-3468
    • Hu, J.1    Miller, M.J.2
  • 57
    • 0033823535 scopus 로고    scopus 로고
    • Evaluation of human anti-mycobacterial immunity using recombinant reporter mycobacteria
    • Kampmann, B., O'Gaora, P., Snewin, V. S, , Gares, M. P., Young, D. B., Levin, M. Evaluation of human anti-mycobacterial immunity using recombinant reporter mycobacteria. J. Infect. Disease, 2000 , 182, 895-901.
    • (2000) J. Infect. Disease , vol.182 , pp. 895-901
    • Kampmann, B.1    O'Gaora, P.2    Snewin, V.S.3    Gares, M.P.4    Young, D.B.5    Levin, M.6
  • 58
    • 0035495579 scopus 로고    scopus 로고
    • How can immunology contribute to the control of tuberculosis?
    • Kaufmann, S.H.E. How does immunology contribute to the control of tuberculosis ? Nat. Rev. Immunol. 2001, 1, 20-30. (Pubitemid 33741972)
    • (2001) Nature Reviews Immunology , vol.1 , Issue.1 , pp. 20-30
    • Kaufmann, S.H.E.1
  • 59
    • 0038352097 scopus 로고    scopus 로고
    • The role of Fe-S proteins in sensing and regulation in bacteria
    • DOI 10.1016/S1369-5274(03)00039-0
    • Kiley, P. J.; Beinert, H. The role of Fe-S proteins in sensing and regulation in bacteria. Curr. Opin. Microbiol., 2003, 6, 181-185. (Pubitemid 36628663)
    • (2003) Current Opinion in Microbiology , vol.6 , Issue.2 , pp. 181-185
    • Kiley, P.J.1    Beinert, H.2
  • 60
    • 0035078647 scopus 로고    scopus 로고
    • Antimycobacterial agent based on mRNA encoding human β-defensin 2 enables primary macrophages to restrict growth of Mycobacterium tuberculosis
    • DOI 10.1128/IAI.69.4.2692-2699.2001
    • Kisich, K. O., Heifets, L., Higgins, M., Diamond, G. Antimycobacterial agent based on mRNA encoding human beta-defensin 2 enables primary macrophages to restrict growth of Mycobacterium tuberculosis. Infect. Immun., 2001, 69, 2692-2699. (Pubitemid 32239746)
    • (2001) Infection and Immunity , vol.69 , Issue.4 , pp. 2692-2699
    • Kisich, K.O.1    Heifets, L.2    Higgins, M.3    Diamond, G.4
  • 64
    • 0027230853 scopus 로고
    • Role of iron in regulation of iron virulence genes
    • Litwin, C. M.; Calderwood, S. B. Role of iron in regulation of iron virulence genes. Clin. Microbiol. Rev., 1993, 6, 137-149.
    • (1993) Clin. Microbiol. Rev , vol.6 , pp. 137-149
    • Litwin, C.M.1    Calderwood, S.B.2
  • 65
    • 50849145229 scopus 로고    scopus 로고
    • The Metal- Dependent Regulators FurA and FurB from Mycobacterium Tuberculosis
    • Lucarelli, D., Vasil, M. L., Meyer-Klaucke, W., Pohl, E. The Metal- Dependent Regulators FurA and FurB from Mycobacterium Tuberculosis. Int. J. Mol. Sci., 2008, 9, 1548-1560.
    • (2008) Int. J. Mol. Sci , vol.9 , pp. 1548-1560
    • Lucarelli, D.1    Vasil, M.L.2    Meyer-Klaucke, W.3    Pohl, E.4
  • 66
    • 0016774173 scopus 로고
    • A new group of water soluble iron-binding compounds from Mycobacteria, the exochelins
    • Macham, L. P.; Ratledge, C. A new group of water soluble iron-binding compounds from Mycobacteria, the exochelins. J. Gen. Microbiol., 1975, 89, 379-382.
    • (1975) J. Gen. Microbiol , vol.89 , pp. 379-382
    • MacHam, L.P.1    Ratledge, C.2
  • 68
    • 0031962882 scopus 로고    scopus 로고
    • DNA chips an array of possibilities
    • Marshall, A.; Hodgson, J. DNA chips, an array of possibilities. Nat. Biotechnol., 1998, 16, 27-31.
    • (1998) Nat. Biotechnol , vol.16 , pp. 27-31
    • Marshall, A.1    Hodgson, J.2
  • 70
    • 0030878979 scopus 로고    scopus 로고
    • Iron uptake and intracellular metal transfer in mycobacteria mediated by xenosiderophores
    • DOI 10.1023/A:1018351728081
    • Matzanke, B. F.; Böhnke, R.; Möllmann, U.; Reissbrodt, R.; Schünemann, V.; Trautwein, A. X. Iron uptake and intracellular metal transfer in mycobacteria mediated by xenosiderophores. Biometals, 1997, 10, 193-203. (Pubitemid 27313623)
    • (1997) BioMetals , vol.10 , Issue.3 , pp. 193-203
    • Matzanke, B.F.1    Bohnke, R.2    Mollmann, U.3    Reissbrodt, R.4    Schunemann, V.5    Trautwein, A.X.6
  • 71
    • 0034528573 scopus 로고    scopus 로고
    • In vivo veritas: The search for TB drug targets goes live
    • DOI 10.1038/82142
    • McKinney, J. D. In vivo veritas: the search for TB drug targets goes live. Nat. Med., 2000, 6, 1330-1333. (Pubitemid 32001015)
    • (2000) Nature Medicine , vol.6 , Issue.12 , pp. 1330-1333
    • McKinney, J.D.1
  • 72
    • 14844318615 scopus 로고    scopus 로고
    • Analyzing Mycobacterium tuberculosis proteomes for candidate vaccine epitopes
    • DOI 10.1016/j.tube.2004.09.005
    • McMurry, J.; Sbai, H.; Gennaro, M. L.; Carter, E. J.; Martin, W.; De Groot, A. S. Analyzing Mycobacterium tuberculosis proteomes for candidate vaccine epitopes. Tuberculosis, 2005, 85, 95-105. (Pubitemid 40431321)
    • (2005) Tuberculosis , vol.85 , Issue.SPEC.ISS. , pp. 95-105
    • McMurry, J.1    Sbai, H.2    Gennaro, M.L.3    Carter, E.J.4    Martin, W.5    De Groot, A.S.6
  • 73
    • 38949111009 scopus 로고    scopus 로고
    • Sphingosine kinase, phosphatidylinositol 3-kinase, Akt, NF-kappaB, and p300 are required for CCL5 production in Mycobacterium bovis Bacillus Calmette-Guérin (BCG)-infected epithelial cells
    • Méndez-Samperio, P.; Pérez, A.; Trejo, A. Sphingosine kinase, phosphatidylinositol 3-kinase, Akt, NF-kappaB, and p300 are required for CCL5 production in Mycobacterium bovis Bacillus Calmette-Guérin (BCG)-infected epithelial cells. Cell Immunol., 2007, 249, 94-100.
    • (2007) Cell Immunol , vol.249 , pp. 94-100
    • Méndez-Samperio, P.1    Pérez, A.2    Trejo, A.3
  • 74
    • 35649024834 scopus 로고    scopus 로고
    • Targeting iron acquisition by Mycobacterium tuberculosis
    • DOI 10.2174/187152607782110031
    • Monfelli, R. R.; Beeson, C. Targeting iron acquisition by Mycobacterium tuberculosis. Infect. Disord. drug Targets, 2007, 7, 213-220. (Pubitemid 350028054)
    • (2007) Infectious Disorders - Drug Targets , vol.7 , Issue.3 , pp. 213-220
    • Monfeli, R.R.1    Beeson, C.2
  • 75
    • 0037415722 scopus 로고    scopus 로고
    • SufC: An unorthodox cytoplasmic ABC/ATPase required for [Fe-S] biogenesis under oxidative stress
    • DOI 10.1093/emboj/cdg061
    • Nachin, L. et al. SufC, an unorthodox cytoplasmic ABC/ATPase required for [Fe-S] biogenesis under oxidative stress. EMBO J. 2003, 22, 427-437. (Pubitemid 36193588)
    • (2003) EMBO Journal , vol.22 , Issue.3 , pp. 427-437
    • Nachin, L.1    Loiseau, L.2    Expert, D.3    Barras, F.4
  • 76
    • 0019348762 scopus 로고
    • Microbial iron compounds
    • Neilands, J.B. Microbial iron compounds. Annu. Rev. Biochem., 1981, 50, 715-731.
    • (1981) Annu. Rev. Biochem , vol.50 , pp. 715-731
    • Neilands, J.B.1
  • 77
    • 0020346483 scopus 로고
    • Microbial envelope proteins related to iron
    • Neilands, J. B. Microbial envelope proteins related to iron. Annu. Rev. Microbiol., 1982, 36, 285-309.
    • (1982) Annu. Rev. Microbiol , vol.36 , pp. 285-309
    • Neilands, J.B.1
  • 78
    • 0025278585 scopus 로고
    • Control of Escherichia coli superoxide dismutase (sodA and sodB) genes by the ferric uptake regulation (fur) locus
    • Niederhoffer, E. C.; Naranjo, C. M.; Bradley, K. L.; Fee, J. A. Control of Escherichia coli superoxide dismutase (sodA and sodB) genes by the ferric uptake regulator (fur) locus. J. Bacteriol., 1990, 172, 1930-1938. (Pubitemid 20112014)
    • (1990) Journal of Bacteriology , vol.172 , Issue.4 , pp. 1930-1938
    • Niederhoffer, E.C.1    Naranjo, C.M.2    Bradley, K.L.3    Fee, J.A.4
  • 79
    • 0036786304 scopus 로고    scopus 로고
    • Construction and characterization of transposon insertion mutations in Corynbacterium diphtheriae that affect expression of the diphtheria toxin repressor (DtxR)
    • Oram, D. M.; Avdalovic, A.; Holmes, R. K. Construction and characterization of transposon insertion mutations in Corynbacterium diphtheriae that affect expression of the diphtheria toxin repressor (DtxR). J. Bacteriol., 2002, 184, 5723-5732.
    • (2002) J. Bacteriol , vol.184 , pp. 5723-5732
    • Oram, D.M.1    Avdalovic, A.2    Holmes, R.K.3
  • 80
    • 2442567822 scopus 로고    scopus 로고
    • A suf operon requirement for Fe-S cluster assembly during iron starvation in Escherichia coli
    • DOI 10.1111/j.1365-2958.2004.04025.x
    • Outten, F. W. et al. A suf operon requirement for Fe-S cluster assembly during iron starvation in Escherichia coli. Mol. Microbiol., 2004, 52, 861-872 (Pubitemid 38621754)
    • (2004) Molecular Microbiology , vol.52 , Issue.3 , pp. 861-872
    • Outten, F.W.1    Djaman, O.2    Storz, G.3
  • 81
    • 0024469919 scopus 로고
    • Iron and virulence in Shigella
    • Payne, S. M. Iron and virulence in shigella. Mol. Microbiol., 1989, 3, 1301-1306. (Pubitemid 19239974)
    • (1989) Molecular Microbiology , vol.3 , Issue.9 , pp. 1301-1306
    • Payne, S.M.1
  • 82
    • 0035838272 scopus 로고    scopus 로고
    • Inflammation and lymphocyte activation during mycobacterial infection in the interferon-γ-deficient mouse
    • DOI 10.1006/cimm.2001.1819
    • Pearl, J. E.; Saunders, B.; Ehlers, S.; Orme, I. M.; Cooper, A. M. Inflammation and lymphocyte activation during mycobacterial infection in the interferon- deficient mouse. Cell Immunol., 2001, 211, 43-50. (Pubitemid 32917757)
    • (2001) Cellular Immunology , vol.211 , Issue.1 , pp. 43-50
    • Pearl, J.E.1    Saunders, B.2    Ehlers, S.3    Orme, I.M.4    Cooper, A.M.5
  • 83
    • 18944366215 scopus 로고    scopus 로고
    • Mechanisms of disease: The role of hepcidin in iron homeostasis - Implications for hemochromatosis and other disorders
    • DOI 10.1038/ncpgasthep0019
    • Pietrangelo, A.; Trautwein, C. Mechanism of disease , the role of hepcidin in iron homeostasis-implications for hemochromatosis and other disorders. Nat. Clin. Pract. Gastroenterol. Hepato., 2004, 1, 39-45. (Pubitemid 40823692)
    • (2004) Nature Clinical Practice Gastroenterology and Hepatology , vol.1 , Issue.1 , pp. 39-45
    • Pietrangelo, A.1    Trautwein, C.2
  • 84
    • 19544383636 scopus 로고    scopus 로고
    • Computational prediction and experimental verification of novel IdeR binding sites in the upstream sequences of Mycobacterium tuberculosis open reading frames
    • DOI 10.1093/bioinformatics/bti375
    • Prakash, P; Yellaboina, S.; Ranjan, A.; Hasnain, S. E. Computational prediction and experimental verification of novel IdeR binding sites in the upstream sequences of Mycobacterium tuberculosis ORFs. Bioinformatics, 2005, 21, 2161-2166. (Pubitemid 40731565)
    • (2005) Bioinformatics , vol.21 , Issue.10 , pp. 2161-2166
    • Prakash, P.1    Yellaboina, S.2    Ranjan, A.3    Hasnain, S.E.4
  • 85
    • 0036718574 scopus 로고    scopus 로고
    • Identification of a DtxR-regulated operon that is essential for siderophore dependent iron uptake in Corynbacterium diphtheriae
    • Qian, Y.; Lee, J. H.; Holmes, R. K. Identification of a DtxR-regulated operon that is essential for siderophore dependent iron uptake in Corynbacterium diphtheriae. J. Bacteriol., 2002, 184, 4846-4856.
    • (2002) J. Bacteriol , vol.184 , pp. 4846-4856
    • Qian, Y.1    Lee, J.H.2    Holmes, R.K.3
  • 86
    • 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.; Sello, J.; Keating, T. A.; Weinreb, P. H.; Walsh, C. T. Identification of Mycobacterium tuberculosis gene cluster encoding the biosynthetic enzymes for assembly of the virulence conferring siderophore mycobactin. Chem. Biol., 1998, 5, 631-645. (Pubitemid 28519450)
    • (1998) Chemistry and Biology , vol.5 , Issue.11 , pp. 631-645
    • Quadri, L.E.N.1    Sello, J.2    Keating, T.A.3    Weinreb, P.H.4    Walsh, C.T.5
  • 87
    • 37849036789 scopus 로고    scopus 로고
    • 5'-O-[(N-acyl)sulfamoyl]adenosines as antitubercular agents that inhibit MbtA: An adenylation enzyme required for siderophore biosynthesis of the mycobactins
    • Qiao C.; Gupte, A.; Boshoff, H. I.; Wilson, D. J.; Bennett, E.M.; Somu, R. V.; Barry III, C. E.; Aldrich, C. C. 5'-O-[(N-acyl)sulfamoyl]adenosines as antitubercular agents that inhibit MbtA: an adenylation enzyme required for siderophore biosynthesis of the mycobactins. J. Med.Chem., 2004, 50(24), 6080-6094.
    • (2004) J. Med.Chem , vol.50 , Issue.24 , pp. 6080-6094
    • Qiao, C.1    Gupte, A.2    Boshoff, H.I.3    Wilson, D.J.4    Bennett, E.M.5    Somu, R.V.6    Iii, B.7    E, C.8    Aldrich, C.C.9
  • 88
    • 0027331982 scopus 로고
    • Effect of iron on growth and siderophore production of mycobacteria
    • Raghu, B.; Sarma, G. R.; Venkatesan, P. Effect of iron on growth and siderophore production of mycobacteria. Biochem. Mol. Bio. Int., 1993, 31, 341-348.
    • (1993) Biochem. Mol. Bio. Int , vol.31 , pp. 341-348
    • Raghu, B.1    Sarma, G.R.2    Venkatesan, P.3
  • 89
    • 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, K.K.; Babu, C. R. Inhibition of the in-vitro growth of Mycobacterium tuberculosis by a phytosiderophore. J. Med. Microbiol., 2001, 50, 916-918. (Pubitemid 32905221)
    • (2001) Journal of Medical Microbiology , vol.50 , Issue.10 , pp. 916-918
    • Rajiv, J.1    Dam, T.2    Kumar, S.3    Bose, M.4    Aggarwal, K.K.5    Babu, C.R.6
  • 90
    • 33646805366 scopus 로고    scopus 로고
    • IdeR in Mycobacteria, from target recognition to physiological function
    • Ranjan, S.; Yellabona, S.; Ranjan, A. IdeR in Mycobacteria, from target recognition to physiological function. Critical Revs. Microbiol., 2006, 32, 69-75.
    • (2006) Critical Revs. Microbiol , vol.32 , pp. 69-75
    • Ranjan, S.1    Yellabona, S.2    Ranjan, A.3
  • 91
    • 0001544469 scopus 로고
    • The accumulation of salicylic acid by mycobacteria during growth on iron-deficient medium
    • Ratledge, C.; Winder, F. G. The accumulation of salicylic acid by mycobacteria during growth on iron-deficient medium. Biochem. J. 1962, 84, 501-506.
    • (1962) Biochem. J , vol.84 , pp. 501-506
    • Ratledge, C.1    Winder, F.G.2
  • 92
    • 0020288432 scopus 로고
    • Iron transport in Mycobacterium smegmatis: The location of mycobactin by electron microscopy
    • Ratledge, C.; Patel, P. V.; Mundy J. Iron transport in Mycobacterium smegmatis: the location of mycobactin by electron microscopy. J. Gen. Microbiol. 1982, 128, 1559-1565. (Pubitemid 12013271)
    • (1982) Journal of General Microbiology , vol.128 , Issue.7 , pp. 1559-1565
    • Ratledge, C.1    Patel, P.V.2    Mundy, J.3
  • 94
    • 0347722524 scopus 로고    scopus 로고
    • Iron mycobacteria and tuberculosis
    • Ratledge, C. Iron, mycobacteria and tuberculosis.Tuberculosis, 2004, 84, 110-130.
    • (2004) Tuberculosis , vol.84 , pp. 110-130
    • Ratledge, C.1
  • 95
    • 0037849870 scopus 로고    scopus 로고
    • Analysis of virulence plasmid gene expression of intra-macrophage and in vitro grown Rhodococcus equi ATCC 33701
    • DOI 10.1016/S0378-1135(03)00099-3
    • Ren, J.; Prescott, J. F. Analysis of virulence plasmid gene expression of intra-macrophage and in vitro grown Rhodococcus equi ATCC33701.Vet. Microbiol. 2003, 94, 167-182. (Pubitemid 36627816)
    • (2003) Veterinary Microbiology , vol.94 , Issue.2 , pp. 167-182
    • Ren, J.1    Prescott, J.F.2
  • 96
    • 70349307297 scopus 로고    scopus 로고
    • Phosphate depletion:a novel trigger for M.tuberculosis persistence
    • Rifat, D.; Bishai, W. R.; Karakousis, P.C. Phosphate depletion:a novel trigger for M.tuberculosis persistence.J. Infect. Dis. 2009, 200, 1126-1135.
    • (2009) J. Infect. Dis , vol.200 , pp. 1126-1135
    • Rifat, D.1    Bishai, W.R.2    Karakousis, P.C.3
  • 97
    • 0036081140 scopus 로고    scopus 로고
    • IdeR, an essential gene in Mycobacterium tuberculosis: Role of IdeR in iron-dependent gene expression, iron metabolism, and oxidative stress response
    • DOI 10.1128/IAI.70.7.3371-3381.2002
    • Rodriguez, G.M.;Voskuil, M.I.; Gold, B.; Scoolnik, G. K.; Smith, I. IdeR, an essential gene in Mycobacterium tuberculosis, role of IdeR1 in irondependent gene expression, iron metabolism and oxidative stress response. Infect. Immun. 2002, 70, 3371-3381. (Pubitemid 34665972)
    • (2002) Infection and Immunity , vol.70 , Issue.7 , pp. 3371-3381
    • Rodriguez, G.M.1    Voskuil, M.I.2    Gold, B.3    Schoolnik, G.K.4    Smith, I.5
  • 98
    • 0037344575 scopus 로고    scopus 로고
    • Mechanisms of iron regulation in mycobacteria: Role in physiology and virulence
    • DOI 10.1046/j.1365-2958.2003.03384.x
    • Rodriguez, G. M.; Smith, I. Mechanism of iron regulation in mycobacteria, role in physiology and virulence. Mol. Microbiol., 2003, 47, 1485-1494. (Pubitemid 36363334)
    • (2003) Molecular Microbiology , vol.47 , Issue.6 , pp. 1485-1494
    • Rodriguez, G.M.1    Smith, I.2
  • 99
    • 33745484154 scopus 로고    scopus 로고
    • Control of iron metabolism in Mycobacterium tuberculosis
    • DOI 10.1016/j.tim.2006.05.006, PII S0966842X06001260
    • Rodriguez, G.M. Control of iron metabolism in Mycobacterium tuberculosis. Trends Microbiol., 2006, 14, 320-327. (Pubitemid 43963365)
    • (2006) Trends in Microbiology , vol.14 , Issue.7 , pp. 320-327
    • Rodriguez, G.M.1
  • 100
    • 30744441922 scopus 로고    scopus 로고
    • Identification of an ABC transporter required for iron acquisition and virulence in Mycobacterium tuberculosis
    • DOI 10.1128/JB.188.2.424-430.2006
    • Rodriguez, G. M.; Smith, I. Identification of an ABC transporter required for iron acquisition and virulence in Mycobacterium tuberculosis. J. Bacteriol., 2006, 188, 424-430. (Pubitemid 43100529)
    • (2006) Journal of Bacteriology , vol.188 , Issue.2 , pp. 424-430
    • Rodriguez, G.M.1    Smith, I.2
  • 101
    • 23444457775 scopus 로고    scopus 로고
    • Immune responses to tuberculosis in developing countries: Implications for new vaccines
    • DOI 10.1038/nri1666
    • Rook, G. A. W.; Dheda, K.; Zumla, A. Immune reponse to tuberculosis in developing countries; implications for new vaccines. Nat. Rev. Immunol., 2005, 5, 661-667. (Pubitemid 41113197)
    • (2005) Nature Reviews Immunology , vol.5 , Issue.8 , pp. 661-667
    • Rook, G.A.W.1    Dheda, K.2    Zumla, A.3
  • 103
  • 104
    • 0025809889 scopus 로고
    • Iron dependent regulation of diphtheria toxin and siderophore expression by the cloned Corybacterium diphtheriae repressor gene dtxR in C. diphtheriae C7 strains
    • Schmitt, M. P.; Holmes, R. K. Iron dependent regulation of diphtheria toxin and siderophore expression by the cloned Corybacterium diphtheriae repressor gene dtxR in C. diphtheriae C7 strains. Infect. Immun., 1991, 59, 1899-1904.
    • (1991) Infect. Immun , vol.59 , pp. 1899-1904
    • Schmitt, M.P.1    Holmes, R.K.2
  • 105
    • 0030827610 scopus 로고    scopus 로고
    • Characterization of lipoprotein IRP1 from Corynebacterium diphtheriae, which is regulated by the diphtheria toxin repressor (DtxR) and iron
    • Schmitt, M. P.; Talley, B.G.; Holmes, R. K. Characterization of lipoprotein IRP1 from Corynbacterium diphtheriae, which is regulated by the diphtheria toxin repressor (DtxR) and iron. Infect. Immun., 1997, 65, 5364-5367. (Pubitemid 27513596)
    • (1997) Infection and Immunity , vol.65 , Issue.12 , pp. 5364-5367
    • Schmitt, M.P.1    Talley, B.G.2    Holmes, R.K.3
  • 106
    • 0035032561 scopus 로고    scopus 로고
    • Screening system for xenosiderophores as potential drug delivery agents in mycobacteria
    • DOI 10.1128/AAC.45.5.1317-1322.2001
    • Schumann, G.; Mollman U. Screening system for xenosiderophores as potential drugs/delivery agents in mycobacteria. Antimicrob. Agents Chemother., 2001, 45, 1317-1322. (Pubitemid 32374097)
    • (2001) Antimicrobial Agents and Chemotherapy , vol.45 , Issue.5 , pp. 1317-1322
    • Schumann, G.1    Mollmann, U.2
  • 107
    • 0035186635 scopus 로고    scopus 로고
    • DNA vaccines: Future strategies and relevance to intracellular pathogens
    • DOI 10.1046/j.1440-1711.2001.01044.x
    • Sharma, A. K.; Khuller, G. K. DNA vaccines - future strategies and relevance against intracellular pathogens. Immunol. Cell Biol. 2001, 79, 537-546. (Pubitemid 33070442)
    • (2001) Immunology and Cell Biology , vol.79 , Issue.6 , pp. 537-546
    • Sharma, A.K.1    Khuller, G.K.2
  • 108
    • 0035543652 scopus 로고    scopus 로고
    • Recombinant mycobacterial proteins - A review
    • Sharma, A. K.; Khuller, G. K. Recombinant mycobacterial proteins - A review. Indian J. Exp. Biol., 2001, 39, 1214-1219.
    • (2001) Indian J. Exp. Biol , vol.39 , pp. 1214-1219
    • Sharma, A.K.1    Khuller, G.K.2
  • 109
    • 77956235790 scopus 로고    scopus 로고
    • Cytosolic Iron- Sulfur Assembly (CIA) System: Factors, Mechanism, and Relevance to cellular Iron Regulation
    • Sharma, A. K.; Pallesen, L.; Spang, R. J.; Walden, W. E. Cytosolic Iron- Sulfur Assembly (CIA) System: Factors, Mechanism, and Relevance to cellular Iron Regulation. J. Biol. Chem., 2010, 285, 26745-26751.
    • (2010) J. Biol. Chem. , vol.285 , pp. 26745-26751
    • Sharma, A.K.1    Pallesen, L.2    Spang, R.J.3    Walden, W.E.4
  • 111
    • 70149116303 scopus 로고    scopus 로고
    • Mycobacterium tuberculosis WhiB3 maintains redox homeostasis by regulating virulence lipid anabolism to modulate macrophage response
    • Singh, A.; Crossman, D. K.; Mai, D.; Guidry, L.; Voskuil, M. I.; Renfrow, M. B.; Steyn, A. J. C. Mycobacterium tuberculosis WhiB3 maintains redox homeostasis by regulating virulence lipid anabolism to modulate macrophage response. PLoS Pathog., 2009, 5, 100045.
    • (2009) PLoS Pathog , vol.5 , pp. 100045
    • Singh, A.1    Crossman, D.K.2    Mai, D.3    Guidry, L.4    Voskuil, M.I.5    Renfrow, M.B.6    Steyn, A.J.C.7
  • 112
    • 0000730135 scopus 로고
    • The structure of mycobactin P, a growth factor for Mycobacterium johnei, and the significance of its iron complex
    • Snow, G. A. The structure of mycobactin P, a growth factor for Mycobacterium johnei, and the significance of its iron complex. Biochem J., 1965, 94, 160-165
    • (1965) Biochem J , vol.94 , pp. 160-165
    • Snow, G.A.1
  • 113
    • 0014803645 scopus 로고
    • Mycobactins: Iron-chelating growth factors from mycobacteria
    • Snow, G. A. 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
  • 114
    • 30444445995 scopus 로고    scopus 로고
    • Rationally-designed nucleoside antibiotics that inhibit siderophore biosynthesis of Mycobacterium tuberculosis
    • DOI 10.1021/jm051060o
    • Somu, R. V.; Boshoff, H.; Qiao, C.; Bennett, E. M.; Barry III, C. E.; Aldrich, C. C. Rationally Designed Nucleoside Antibiotics That Inhibit Siderophore Biosynthesis of Mycobacterium tuberculosis. J. Med. Chem., 2006, 49 (1), 31-34. (Pubitemid 43077318)
    • (2006) Journal of Medicinal Chemistry , vol.49 , Issue.1 , pp. 31-34
    • Somu, R.V.1    Boshoff, H.2    Qiao, C.3    Bennett, E.M.4    Barry III, C.E.5    Aldrich, C.C.6
  • 116
    • 0030862226 scopus 로고    scopus 로고
    • Definition of Mycobacterium tuberculosis culture filtrate proteins by two-dimensional polyacrylamide gel electrophoresis, N-terminal amino acid sequencing, and electrospray mass spectrometry
    • Sonnenberg, M. G.; Belisle, J. T. Definition of Mycobacterium tuberculosis culture filtrate proteins by two-dimensional polyacrylamide gel electrophoresis, N-terminal amino-acid sequencing , and electrospray mass spectrometry. Infect. Immunol., 1997, 65, 4515-4524. (Pubitemid 27463220)
    • (1997) Infection and Immunity , vol.65 , Issue.11 , pp. 4515-4524
    • Sonnenberg, M.G.1    Belisle, J.T.2
  • 117
    • 34848888911 scopus 로고    scopus 로고
    • Expression and localization of hepcidin in macrophages: A role in host defense against tuberculosis
    • DOI 10.1189/jlb.0407216
    • Sow, F. B.; Florence, W. C.; Satoskar, A. R.; Schlesinger, L. S.; Zwilling, B. S.; Lafuse, W. P. Expression and localization of hepcidin in macrophages, a role in host defence against tuberculosis. J. Leukoc. Biol., 2007, 82; 934-945. (Pubitemid 47511054)
    • (2007) Journal of Leukocyte Biology , vol.82 , Issue.4 , pp. 934-945
    • Sow, F.B.1    Florence, W.C.2    Satoskar, A.R.3    Schlesinger, L.S.4    Zwilling, B.S.5    Lafuse, W.P.6
  • 119
    • 0037047411 scopus 로고    scopus 로고
    • A third bacterial system for the assembly of iron-sulfur clusters with homologs in Archaea and plastids
    • DOI 10.1074/jbc.C200365200
    • Takahashi, Y.; Tokumoto, U. A third bacterial system for the assembly of iron-sulfur clusters with homologs in archaea and plastids. J. Biol. Chem., 2002, 277, 28380-28383. (Pubitemid 41079260)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.32 , pp. 28380-28383
    • Takahashi, Y.1    Tokumoto, U.2
  • 120
    • 0033985228 scopus 로고    scopus 로고
    • Iron and oxidative stress in bacteria
    • DOI 10.1006/abbi.1999.1518
    • Touati, D. Iron and oxidative stress in bacteria. Arch. Biochem. Biophys., 2000, 373, 1-6. (Pubitemid 30046483)
    • (2000) Archives of Biochemistry and Biophysics , vol.373 , Issue.1 , pp. 1-6
    • Touati, D.1
  • 121
    • 0029164719 scopus 로고
    • Fur regulon of Salmonella typhimurium, identification of new iron regulated genes
    • Tsolis, R. M.; Baumler, A. J., Stojiljkovic, I. Heffron, F. Fur regulon of Salmonella typhimurium, identification of new iron regulated genes. J Bacteriol., 1995, 177, 4628-4637.
    • (1995) J Bacteriol , vol.177 , pp. 4628-4637
    • Tsolis, R.M.1    Baumler, A.J.2    Stojiljkovic, I.3    Heffron, F.4
  • 122
    • 50849096115 scopus 로고    scopus 로고
    • The iron export protein ferroportin 1 is differentially expressed in mouse macrophage populations and is present in the mycobacterial-containing phagosome
    • Van Zandt, K. E.; Sow, F. B.; Florence, W. C.; Zwilling, B. S.; Satoskar, A. R.; Schlesinger, L. S.; Lafuse, W. P. The iron export protein ferroportin 1 is differentially expressed in mouse macrophage populations and is present in the mycobacterial-containing phagosome. J. Leukoc Biol., 2008, 84, 689-700.
    • (2008) J. Leukoc Biol , vol.84 , pp. 689-700
    • Van Zandt, K.E.1    Sow, F.B.2    Florence, W.C.3    Zwilling, B.S.4    Satoskar, A.R.5    Schlesinger, L.S.6    Lafuse, W.P.7
  • 124
    • 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, D.; Lee, B. Y.; Horwitz, M. A.; Gibson, B. Identification of Fur, aconitase and other proteins expressed by Mycobacterium tuberculosis under conditions of low and high concentrations of iron by combined twodimensional gel electrophoresis and mass spectrophotometry. Infect. Immun., 1999, 67, 327-336. (Pubitemid 29021666)
    • (1999) Infection and Immunity , vol.67 , Issue.1 , pp. 327-336
    • Wong, D.K.1    Lee, B.-Y.2    Horwitz, M.A.3    Gibson, B.W.4
  • 125
    • 0032569011 scopus 로고    scopus 로고
    • Total synthesis of mycobactin analogues as potent antimicrobial agents using a minimal protecting group strategy
    • Xu, Y.; Miller, J. J. Total synthesis of mycobactin analogues as potent antimicrobial 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
  • 126
    • 0032557666 scopus 로고    scopus 로고
    • Assembly of iron-sulfur clusters. Identification of an iscSUA-hscBA-fdx gene cluster from Azotobacter vinelandii
    • DOI 10.1074/jbc.273.21.13264
    • Zheng L.; Cash, V. L.; Flint, D. H.; Dean, D. R. Assembly of iron-sulfur clusters.Identification of an iscSUA-hscBA-fdx gene cluster from Azotobacter vinelandii. J. Biol. Chem., 1998, 273, 13264-13272. (Pubitemid 28246899)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.21 , pp. 13264-13272
    • Zheng, L.1    Cash, V.L.2    Flint, D.H.3    Dean, D.R.4
  • 127
    • 0034932337 scopus 로고    scopus 로고
    • DNA microarray-mediated transcriptional profiling of the Escherichia coli response to hydrogen peroxide
    • DOI 10.1128/JB.183.15.4562-4570.2001
    • Zheng, M.; Wang, X.; Templeton, L. J.; Smulski, D. R.; LaRossa, G. S.; Robert A. DNA microarray -mediated transcriptional profiling of the Escherichia coli response to hydrogen peroxide. J. Bacteriol., 2001, 183, 4562-4570. (Pubitemid 32646006)
    • (2001) Journal of Bacteriology , vol.183 , Issue.15 , pp. 4562-4570
    • Zheng, M.1    Wang, X.2    Templeton, L.J.3    Smulski, D.R.4    LaRossa, R.A.5    Storz, G.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.