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Volumn 26, Issue , 2018, Pages 151-183

Sideromycins as Pathogen-Targeted Antibiotics

Author keywords

Albomycin; Antibiotic delivery systems; Baulamycin; Enterobactin; Grisein; Microcin; Mycobactin; Pyoverdine; Salmycin; Sideromycin; Staphyloferrin; Tetroazolemycin; Trojan horse; Xenosiderophore

Indexed keywords

ANTIBIOTIC AGENT; CHORISMIC ACID; CIPROFLOXACIN; DEFEROXAMINE; FERRIC ION; FERRIMYCIN; FERRIMYCIN A1; FERRIMYCIN A2; FERRIMYCIN B; GRISEIN; IRON CHELATE; PETROBACTIN; SALICYLIC ACID; SALMYCIN; SIDEROMYCIN DERIVATIVE; SIDEROPHORE; STAPHYLOFERRIN; TETROAZOLEMYCIN A; TETROAZOLEMYCIN B; UNCLASSIFIED DRUG;

EID: 85023759420     PISSN: 18622461     EISSN: 1862247X     Source Type: Book Series    
DOI: 10.1007/7355_2017_19     Document Type: Chapter
Times cited : (55)

References (188)
  • 2
    • 84955461306 scopus 로고    scopus 로고
    • Antibacterial drug discovery in the resistance era
    • Brown ED, Wright GD (2016) Antibacterial drug discovery in the resistance era. Nature 529:336–343. doi:10.1038/nature17042
    • (2016) Nature , vol.529 , pp. 336-343
    • Brown, E.D.1    Wright, G.D.2
  • 3
    • 85002341700 scopus 로고    scopus 로고
    • New antibiotics from nature’s chemical inventory
    • Wencewicz TA (2016) New antibiotics from nature’s chemical inventory. Bioorg Med Chem 24:6227–6252. doi:10.1016/j.bmc.2016.09.014
    • (2016) Bioorg Med Chem , vol.24 , pp. 6227-6252
    • Wencewicz, T.A.1
  • 4
    • 84951845275 scopus 로고    scopus 로고
    • Targeted treatment for bacterial infections: Prospects for pathogen-specific antibiotics coupled with rapid diagnostics
    • Maxson T, Mitchell DA (2016) Targeted treatment for bacterial infections: prospects for pathogen-specific antibiotics coupled with rapid diagnostics. Tetrahedron 72:3609–3624. doi:10.1016/j.tet.2015.09.069
    • (2016) Tetrahedron , vol.72 , pp. 3609-3624
    • Maxson, T.1    Mitchell, D.A.2
  • 5
    • 64649088018 scopus 로고    scopus 로고
    • Outer membrane permeability and antibiotic resistance
    • Delcour AH (2009) Outer membrane permeability and antibiotic resistance. Biochim Biophys Acta 1794:808–816. doi:10.1016/j.bbapap.2008.11.005
    • (2009) Biochim Biophys Acta , vol.1794 , pp. 808-816
    • Delcour, A.H.1
  • 6
    • 84963979272 scopus 로고    scopus 로고
    • Permeability barrier of Gram-negative cell envelopes and approaches to bypass it
    • Zgurskaya HI, Lopez CA, Gnanakaran S (2015) Permeability barrier of Gram-negative cell envelopes and approaches to bypass it. ACS Infect Dis 1:512–522. doi:10.1021/acsinfecdis. 5b00097
    • (2015) ACS Infect Dis , vol.1 , pp. 512-522
    • Zgurskaya, H.I.1    Lopez, C.A.2    Gnanakaran, S.3
  • 8
    • 84955307030 scopus 로고    scopus 로고
    • Tabtoxinine-β-lactam is a “stealth” β-lactam antibiotic that evades β-lactamase-mediated antibiotic resistance
    • Hart KM, Reck M, Bowman GR, Wencewicz TA (2016) Tabtoxinine-β-lactam is a “stealth” β-lactam antibiotic that evades β-lactamase-mediated antibiotic resistance. Med Chem Commun 7:118–127. doi:10.1039/C5MD00325C
    • (2016) Med Chem Commun , vol.7 , pp. 118-127
    • Hart, K.M.1    Reck, M.2    Bowman, G.R.3    Wencewicz, T.A.4
  • 9
    • 79952578695 scopus 로고    scopus 로고
    • Maximizing the therapeutic window of an antimicrobial drug by imparting mitochondrial sequestration in human cells
    • Pereira MP, Kelley SO (2011) Maximizing the therapeutic window of an antimicrobial drug by imparting mitochondrial sequestration in human cells. J Am Chem Soc 133:3260–3263. doi:10.1021/ja110246u
    • (2011) J am Chem Soc , vol.133 , pp. 3260-3263
    • Pereira, M.P.1    Kelley, S.O.2
  • 10
    • 0033598377 scopus 로고    scopus 로고
    • Glycosylation of fluoroquinolones through direct and oxygenated polymethylene linkages as a sugar-mediated active transport system for antimicrobials
    • Jung ME, Yang EC, Vu BT, Kiankarimi M, Spyrou E, Kaunitz J (1999) Glycosylation of fluoroquinolones through direct and oxygenated polymethylene linkages as a sugar-mediated active transport system for antimicrobials. J Med Chem 42:3899–3909. doi:10.1021/jm990015b
    • (1999) J Med Chem , vol.42 , pp. 3899-3909
    • Jung, M.E.1    Yang, E.C.2    Vu, B.T.3    Kiankarimi, M.4    Spyrou, E.5    Kaunitz, J.6
  • 11
    • 84940556588 scopus 로고    scopus 로고
    • An efficient system for intracellular delivery of beta-lactam antibiotics to overcome bacterial resistance
    • Abed N, Said-Hassane F, Zouhiri F, Mougin J, Nicolas V, Desmaele D, Gref R, Couvreur P (2015) An efficient system for intracellular delivery of beta-lactam antibiotics to overcome bacterial resistance. Sci Rep 5:13500. doi:10.1038/srep13500
    • (2015) Sci Rep , vol.5
    • Abed, N.1    Said-Hassane, F.2    Zouhiri, F.3    Mougin, J.4    Nicolas, V.5    Desmaele, D.6    Gref, R.7    Couvreur, P.8
  • 12
    • 84919698126 scopus 로고    scopus 로고
    • Antibiotic-containing polymers for localized, sustained drug delivery
    • Stebbins ND, Ouimet MA, Uhrich KE (2014) Antibiotic-containing polymers for localized, sustained drug delivery. Adv Drug Deliv Rev 78:77–87. doi:10.1016/j.addr.2014.04.006
    • (2014) Adv Drug Deliv Rev , vol.78 , pp. 77-87
    • Stebbins, N.D.1    Ouimet, M.A.2    Uhrich, K.E.3
  • 15
    • 0034044581 scopus 로고    scopus 로고
    • Studies and syntheses of siderophores, microbial iron chelators, and analogs as potential drug delivery agents
    • Roosenberg II JM, Lin YM, Lu Y, Miller MJ (2000) Studies and syntheses of siderophores, microbial iron chelators, and analogs as potential drug delivery agents. Curr Med Chem 7:159–197. doi:10.2174/0929867003375353
    • (2000) Curr Med Chem , vol.7 , pp. 159-197
    • Roosenberg, J.M.1    Lin, Y.M.2    Lu, Y.3    Miller, M.J.4
  • 17
    • 75949092121 scopus 로고    scopus 로고
    • Anti-virulence strategies to combat bacteria-mediated disease
    • Rasko DA, Sperandio V (2010) Anti-virulence strategies to combat bacteria-mediated disease. Nat Rev Drug Discov 9:117–128. doi:10.1038/nrd3013
    • (2010) Nat Rev Drug Discov , vol.9 , pp. 117-128
    • Rasko, D.A.1    Sperandio, V.2
  • 19
    • 85000838210 scopus 로고    scopus 로고
    • Transition metals and virulence in bacteria
    • Palmer LD, Skaar EP (2016) Transition metals and virulence in bacteria. Annu Rev Genet 50:67–91. doi:10.1146/annurev-genet-120215-035146
    • (2016) Annu Rev Genet , vol.50 , pp. 67-91
    • Palmer, L.D.1    Skaar, E.P.2
  • 20
    • 77958143617 scopus 로고    scopus 로고
    • The battle for iron between bacterial pathogens and their vertebrate hosts
    • Skaar EP (2010) The battle for iron between bacterial pathogens and their vertebrate hosts. PLoS Pathog 6:e1000949. doi:10.1371/journal.ppat.1000949
    • (2010) Plos Pathog , vol.6
    • Skaar, E.P.1
  • 21
    • 84963769435 scopus 로고    scopus 로고
    • Bacterial ferrous iron transport: The Feo system
    • Lau CK, Krewulak KD, Vogel HJ (2016) Bacterial ferrous iron transport: the Feo system. FEMS Microbiol Rev 40:273–298. doi:10.1093/femsre/fuv049
    • (2016) FEMS Microbiol Rev , vol.40 , pp. 273-298
    • Lau, C.K.1    Krewulak, K.D.2    Vogel, H.J.3
  • 22
    • 84889573712 scopus 로고    scopus 로고
    • Bacterial receptors for host transferrin and lactoferrin: Molecular mechanisms and role in host-microbe interactions
    • Morgenthau A, Pogoutse A, Adamiak P, Moraes TF, Schryvers AB (2013) Bacterial receptors for host transferrin and lactoferrin: molecular mechanisms and role in host-microbe interactions. Future Microbiol 8:1575–1585. doi:10.2217/fmb.13.125
    • (2013) Future Microbiol , vol.8 , pp. 1575-1585
    • Morgenthau, A.1    Pogoutse, A.2    Adamiak, P.3    Moraes, T.F.4    Schryvers, A.B.5
  • 24
    • 77951981537 scopus 로고    scopus 로고
    • Chemistry and biology of siderophores
    • Hider RC, Kong X (2010) Chemistry and biology of siderophores. Nat Prod Rep 27:637–657. doi:10.1039/b906679a
    • (2010) Nat Prod Rep , vol.27 , pp. 637-657
    • Hider, R.C.1    Kong, X.2
  • 25
    • 84931074436 scopus 로고    scopus 로고
    • Diverging roles of bacterial siderophores during infection
    • Holden VI, Bachman MA (2015) Diverging roles of bacterial siderophores during infection. Metallomics 7:986–995. doi:10.1039/c4mt00333k
    • (2015) Metallomics , vol.7 , pp. 986-995
    • Holden, V.I.1    Bachman, M.A.2
  • 26
    • 67651244131 scopus 로고    scopus 로고
    • Siderocalins: Siderophore-binding proteins of the innate immune system
    • Clifton MC, Corrent C, Strong RK (2009) Siderocalins: siderophore-binding proteins of the innate immune system. Biometals 22:557–564. doi:10.1007/s10534-009-9207-6
    • (2009) Biometals , vol.22 , pp. 557-564
    • Clifton, M.C.1    Corrent, C.2    Strong, R.K.3
  • 28
    • 85002835024 scopus 로고    scopus 로고
    • Human metabolome-derived cofactors are required for the antibacterial activity of siderocalin in urine
    • Shields-Cutler RR, Crowley JR, Miller CD, Stapleton AE, Cui W, Henderson JP (2016) Human metabolome-derived cofactors are required for the antibacterial activity of siderocalin in urine. J Biol Chem 291:25901–25910. doi:10.1074/jbc.M116.759183
    • (2016) J Biol Chem , vol.291 , pp. 25901-25910
    • Shields-Cutler, R.R.1    Crowley, J.R.2    Miller, C.D.3    Stapleton, A.E.4    Cui, W.5    Henderson, J.P.6
  • 30
    • 33748051446 scopus 로고    scopus 로고
    • Microbial evasion of the immune system: Structural modifications of enterobactin impair siderocalin recognition
    • Abergel RJ, Moore EG, Strong RK, Raymond KN (2006) Microbial evasion of the immune system: structural modifications of enterobactin impair siderocalin recognition. J Am Chem Soc 128:10998–10999. doi:10.1021/ja062476+
    • (2006) J am Chem Soc , vol.128 , pp. 10998-10999
    • Abergel, R.J.1    Moore, E.G.2    Strong, R.K.3    Raymond, K.N.4
  • 31
    • 33646593180 scopus 로고    scopus 로고
    • How pathogenic bacteria evade mammalian sabotage in the battle for iron
    • Fischbach MA, Lin H, Liu DR, Walsh CT (2006) How pathogenic bacteria evade mammalian sabotage in the battle for iron. Nat Chem Biol 2:132–138. doi:10.1038/nchembio771
    • (2006) Nat Chem Biol , vol.2 , pp. 132-138
    • Fischbach, M.A.1    Lin, H.2    Liu, D.R.3    Walsh, C.T.4
  • 34
    • 84930225222 scopus 로고    scopus 로고
    • Breaking a pathogen’s iron will: Inhibiting siderophore production as an antimicrobial strategy
    • Lamb AL (2015) Breaking a pathogen’s iron will: inhibiting siderophore production as an antimicrobial strategy. Biochim Biophys Acta 1854:1054–1070. doi:10.1016/j.bbapap.2015. 05.001
    • (2015) Biochim Biophys Acta , vol.1854 , pp. 1054-1070
    • Lamb, A.L.1
  • 35
    • 84875696130 scopus 로고    scopus 로고
    • Non-nucleoside inhibitors of BasE, an adenylating enzyme in the siderophore biosynthetic pathway of the opportunistic pathogen Acinetobacter baumannii
    • Neres J, Engelhart CA, Drake EJ, Wilson DJ, Fu P, Boshoff HI, Barry 3rd CE, Gulick AM, Aldrich CC (2013) Non-nucleoside inhibitors of BasE, an adenylating enzyme in the siderophore biosynthetic pathway of the opportunistic pathogen Acinetobacter baumannii. J Med Chem 56:2385–2405. doi:10.1021/jm301709s
    • (2013) J Med Chem , vol.56 , pp. 2385-2405
    • Neres, J.1    Engelhart, C.A.2    Drake, E.J.3    Wilson, D.J.4    Fu, P.5    Boshoff, H.I.6    Barry, C.E.7    Gulick, A.M.8    Aldrich, C.C.9
  • 37
    • 84996866505 scopus 로고    scopus 로고
    • Inhibition of the flavin-dependent monooxygenase siderophore A (SidA) blocks siderophore biosynthesis and aspergillus fumigatus growth
    • Martín del Campo JS, Vogelaar N, Tolani K, Kizjakina K, Harich K, Sobrado P (2016) Inhibition of the flavin-dependent monooxygenase siderophore A (SidA) blocks siderophore biosynthesis and aspergillus fumigatus growth. ACS Chem Biol 11:3035–3042. doi:10.1021/acschembio.6b00666
    • (2016) ACS Chem Biol , vol.11 , pp. 3035-3042
    • Martín Del Campo, J.S.1    Vogelaar, N.2    Tolani, K.3    Kizjakina, K.4    Harich, K.5    Sobrado, P.6
  • 39
    • 0037073693 scopus 로고    scopus 로고
    • The antibiotic activity of N-pentylpantothenamide results from its conversion to ethyldethia-coenzyme A, a coenzyme A antimetabolite
    • Strauss E, Begley TP (2002) The antibiotic activity of N-pentylpantothenamide results from its conversion to ethyldethia-coenzyme A, a coenzyme A antimetabolite. J Biol Chem 277:48205–48209. doi:10.1074/jbc.M204560200
    • (2002) J Biol Chem , vol.277 , pp. 48205-48209
    • Strauss, E.1    Begley, T.P.2
  • 42
    • 0348141912 scopus 로고    scopus 로고
    • Role of siderophore biosynthesis in virulence of Staphylococcus aureus: Identification and characterization of genes involved in production of a siderophore
    • Dale SE, Doherty-Kirby A, Lajoie G, Heinrichs DE (2004) Role of siderophore biosynthesis in virulence of Staphylococcus aureus: identification and characterization of genes involved in production of a siderophore. Infect Immun 72:29–37. doi:10.1128/IAI.72.1.29-37.2004
    • (2004) Infect Immun , vol.72 , pp. 29-37
    • Dale, S.E.1    Doherty-Kirby, A.2    Lajoie, G.3    Heinrichs, D.E.4
  • 45
    • 0016591187 scopus 로고
    • The effect of p-aminosalicyclic acid on iron transport and assimilation in mycobacteria
    • Brown KA, Ratledge C (1975) The effect of p-aminosalicyclic acid on iron transport and assimilation in mycobacteria. Biochim Biophys Acta 385:207–220
    • (1975) Biochim Biophys Acta , vol.385 , pp. 207-220
    • Brown, K.A.1    Ratledge, C.2
  • 46
    • 0345492332 scopus 로고    scopus 로고
    • Synergy and contingency as driving forces for the evolution of multiple secondary metabolite production by Streptomyces species
    • Challis GL, Hopwood DA (2003) Synergy and contingency as driving forces for the evolution of multiple secondary metabolite production by Streptomyces species. Proc Natl Acad Sci U S A 100:14555–14561. doi:10.1073/pnas.1934677100
    • (2003) Proc Natl Acad Sci U S A , vol.100 , pp. 14555-14561
    • Challis, G.L.1    Hopwood, D.A.2
  • 47
    • 0032569011 scopus 로고    scopus 로고
    • Total syntheses of mycobactin analogues as potent antimycobacterial agents using a minimal protecting group strategy
    • Xu Y, Miller MJ (1998) Total syntheses of mycobactin analogues as potent antimycobacterial agents using a minimal protecting group strategy. J Org Chem 63:4314–4322. doi:10.1021/jo980063o
    • (1998) J Org Chem , vol.63 , pp. 4314-4322
    • Xu, Y.1    Miller, M.J.2
  • 48
    • 84865694055 scopus 로고    scopus 로고
    • Syntheses of mycobactin analogs as potent and selective inhibitors of Mycobacterium tuberculosis
    • Juarez-Hernandez RE, Franzblau SG, Miller MJ (2012) Syntheses of mycobactin analogs as potent and selective inhibitors of Mycobacterium tuberculosis. Org Biomol Chem 10:7584–7593. doi:10.1039/c2ob26077h
    • (2012) Org Biomol Chem , vol.10 , pp. 7584-7593
    • Juarez-Hernandez, R.E.1    Franzblau, S.G.2    Miller, M.J.3
  • 50
    • 84899769431 scopus 로고    scopus 로고
    • Inhibitors of TonB function identified by a high-throughput screen for inhibitors of iron acquisition in uropathogenic Escherichia coli CFT073
    • Yep A, McQuade T, Kirchhoff P, Larsen M, Mobley HLT (2014) Inhibitors of TonB function identified by a high-throughput screen for inhibitors of iron acquisition in uropathogenic Escherichia coli CFT073. MBio 5:e01089–e01013. doi:10.1128/mBio.01089-13
    • (2014) Mbio , vol.5 , pp. 89
    • Yep, A.1    McQuade, T.2    Kirchhoff, P.3    Larsen, M.4    Mobley, H.L.T.5
  • 51
    • 84959179863 scopus 로고    scopus 로고
    • High-throughput screening assay for inhibitors of TonB-dependent iron transport
    • Hanson M, Jordan LD, Shipelskiy Y, Newton SM, Klebba PE (2016) High-throughput screening assay for inhibitors of TonB-dependent iron transport. J Biomol Screen 21:316–322. doi:10.1177/1087057115613788
    • (2016) J Biomol Screen , vol.21 , pp. 316-322
    • Hanson, M.1    Jordan, L.D.2    Shipelskiy, Y.3    Newton, S.M.4    Klebba, P.E.5
  • 54
    • 34548082362 scopus 로고    scopus 로고
    • Inhibition of the bacterial heme oxygenases from Pseudomonas aeruginosa and Neisseria meningitidis: Novel antimicrobial targets
    • Furci LM, Lopes P, Eakanunkul S, Zhong S, MacKerell AD, Wilks A (2007) Inhibition of the bacterial heme oxygenases from Pseudomonas aeruginosa and Neisseria meningitidis: novel antimicrobial targets. J Med Chem 50:3804–3813. doi:10.1021/jm0700969
    • (2007) J Med Chem , vol.50 , pp. 3804-3813
    • Furci, L.M.1    Lopes, P.2    Eakanunkul, S.3    Zhong, S.4    Mackerell, A.D.5    Wilks, A.6
  • 57
    • 84996528987 scopus 로고    scopus 로고
    • Siderophore vaccine conjugates protect against uropathogenic Escherichia coli urinary tract infection
    • Mike LA, Smith SN, Sumner CA, Eaton KA, Mobley HL (2016) Siderophore vaccine conjugates protect against uropathogenic Escherichia coli urinary tract infection. Proc Natl Acad Sci U S A 113:13468–13473. doi:10.1073/pnas.1606324113
    • (2016) Proc Natl Acad Sci U S A , vol.113 , pp. 13468-13473
    • Mike, L.A.1    Smith, S.N.2    Sumner, C.A.3    Eaton, K.A.4    Mobley, H.L.5
  • 59
    • 0023227280 scopus 로고
    • Passive immunization with antibodies against iron-regulated outer membrane proteins protects turkeys from Escherichia coli septicemia
    • Bolin CA, Jensen AE (1987) Passive immunization with antibodies against iron-regulated outer membrane proteins protects turkeys from Escherichia coli septicemia. Infect Immun 55:1239–1242
    • (1987) Infect Immun , vol.55 , pp. 1239-1242
    • Bolin, C.A.1    Jensen, A.E.2
  • 60
    • 0037159106 scopus 로고    scopus 로고
    • A laboratory study of an inactivated bivalent iron restricted Salmonella enterica serovars Enteritidis and Typhimurium dual vaccine against Typhimurium challenge in chickens
    • Clifton-Hadley FA, Breslin M, Venables LM, Sprigings KA, Cooles SW, Houghton S, Woodward MJ (2002) A laboratory study of an inactivated bivalent iron restricted Salmonella enterica serovars Enteritidis and Typhimurium dual vaccine against Typhimurium challenge in chickens. Vet Microbiol 89:167–179. doi:10.1016/S0378-1135(02)00169-4
    • (2002) Vet Microbiol , vol.89 , pp. 167-179
    • Clifton-Hadley, F.A.1    Breslin, M.2    Venables, L.M.3    Sprigings, K.A.4    Cooles, S.W.5    Houghton, S.6    Woodward, M.J.7
  • 61
    • 84884264246 scopus 로고    scopus 로고
    • Immunization with the yersiniabactin receptor, FyuA, protects against pyelonephritis in a murine model of urinary tract infection
    • Brumbaugh AR, Smith SN, Mobley HL (2013) Immunization with the yersiniabactin receptor, FyuA, protects against pyelonephritis in a murine model of urinary tract infection. Infect Immun 81:3309–3316. doi:10.1128/iai.00470-13
    • (2013) Infect Immun , vol.81 , pp. 3309-3316
    • Brumbaugh, A.R.1    Smith, S.N.2    Mobley, H.L.3
  • 64
    • 0036280341 scopus 로고    scopus 로고
    • Genetics and assembly line enzymology of siderophore biosynthesis in bacteria
    • Crosa JH, Walsh CT (2002) Genetics and assembly line enzymology of siderophore biosynthesis in bacteria. Microbiol Mol Biol Rev 66:223–249. doi:10.1128/MMBR.66.2.223-249.2002
    • (2002) Microbiol Mol Biol Rev , vol.66 , pp. 223-249
    • Crosa, J.H.1    Walsh, C.T.2
  • 65
    • 38649110468 scopus 로고    scopus 로고
    • Terephthalamide-containing ligands: Fast removal of iron from transferrin
    • Abergel RJ, Raymond KN (2008) Terephthalamide-containing ligands: fast removal of iron from transferrin. J Biol Inorg Chem 13:229–240. doi:10.1007/s00775-007-0314-y
    • (2008) J Biol Inorg Chem , vol.13 , pp. 229-240
    • Abergel, R.J.1    Raymond, K.N.2
  • 66
    • 84941686963 scopus 로고    scopus 로고
    • Coordination chemistry of microbial iron transport
    • Raymond KN, Allred BE, Sia AK (2015) Coordination chemistry of microbial iron transport. Acc Chem Res 48:2496–2505. doi:10.1021/acs.accounts.5b00301
    • (2015) Acc Chem Res , vol.48 , pp. 2496-2505
    • Raymond, K.N.1    Allred, B.E.2    Sia, A.K.3
  • 67
    • 84875454942 scopus 로고    scopus 로고
    • Trihydroxamate siderophore-fluoroquinolone conjugates are selective sideromycin antibiotics that target Staphylococcus aureus
    • Wencewicz TA, Long TE, M€ollmann U, Miller MJ (2013) Trihydroxamate siderophore-fluoroquinolone conjugates are selective sideromycin antibiotics that target Staphylococcus aureus. Bioconjug Chem 24:473–486. doi:10.1021/bc300610f
    • (2013) Bioconjug Chem , vol.24 , pp. 473-486
    • Wencewicz, T.A.1    Long, T.E.2    M€Ollmann, U.3    Miller, M.J.4
  • 68
    • 0037317173 scopus 로고    scopus 로고
    • Acquisition of siderophores in Gram-negative bacteria
    • Faraldo-Gomez JD, Sansom MS (2003) Acquisition of siderophores in Gram-negative bacteria. Nat Rev Mol Cell Biol 4:105–116. doi:10.1038/nrm1015
    • (2003) Nat Rev Mol Cell Biol , vol.4 , pp. 105-116
    • Faraldo-Gomez, J.D.1    Sansom, M.S.2
  • 69
    • 84896719872 scopus 로고    scopus 로고
    • Transcriptional regulation by ferric uptake regulator (Fur) in pathogenic bacteria
    • Troxell B, Hassan HM (2013) Transcriptional regulation by ferric uptake regulator (Fur) in pathogenic bacteria. Front Cell Infect Microbiol 3:59. doi:10.3389/fcimb.2013.00059
    • (2013) Front Cell Infect Microbiol , vol.3
    • Troxell, B.1    Hassan, H.M.2
  • 70
    • 78649685479 scopus 로고    scopus 로고
    • An efflux pump is involved in secretion of newly synthesized siderophore by Pseudomonas aeruginosa
    • Hannauer M, Yeterian E, Martin LW, Lamont IL, Schalk IJ (2010) An efflux pump is involved in secretion of newly synthesized siderophore by Pseudomonas aeruginosa. FEBS Lett 584:4751–4755. doi:10.1016/j.febslet.2010.10.051
    • (2010) FEBS Lett , vol.584 , pp. 4751-4755
    • Hannauer, M.1    Yeterian, E.2    Martin, L.W.3    Lamont, I.L.4    Schalk, I.J.5
  • 71
    • 77749270483 scopus 로고    scopus 로고
    • The ferrichrome uptake pathway in Pseudomonas aeruginosa involves an iron release mechanism with acylation of the siderophore and recycling of the modified desferrichrome
    • Hannauer M, Barda Y, Mislin GLA, Shanzer A, Schalk IJ (2010) The ferrichrome uptake pathway in Pseudomonas aeruginosa involves an iron release mechanism with acylation of the siderophore and recycling of the modified desferrichrome. J Bacteriol 192:1212–1220. doi:10.1128/jb.01539-09
    • (2010) J Bacteriol , vol.192 , pp. 1212-1220
    • Hannauer, M.1    Barda, Y.2    Mislin, G.L.A.3    Shanzer, A.4    Schalk, I.J.5
  • 72
    • 0032545324 scopus 로고    scopus 로고
    • Siderophore-mediated iron transport: Crystal structure of FhuA with bound lipopolysaccharide
    • Ferguson AD, Hofmann E, Coulton JW, Diederichs K, Welte W (1998) Siderophore-mediated iron transport: crystal structure of FhuA with bound lipopolysaccharide. Science 282:2215–2220
    • (1998) Science , vol.282 , pp. 2215-2220
    • Ferguson, A.D.1    Hofmann, E.2    Coulton, J.W.3    Diederichs, K.4    Welte, W.5
  • 74
    • 77956505672 scopus 로고    scopus 로고
    • TonB-dependent transporters: Regulation, structure, and function
    • Noinaj N, Guillier M, Barnard TJ, Buchanan SK (2010) TonB-dependent transporters: regulation, structure, and function. Annu Rev Microbiol 64:43–60. doi:10.1146/annurev. micro.112408.134247
    • (2010) Annu Rev Microbiol , vol.64 , pp. 43-60
    • Noinaj, N.1    Guillier, M.2    Barnard, T.J.3    Buchanan, S.K.4
  • 75
    • 84867670628 scopus 로고    scopus 로고
    • Structure of AMP-PNP-bound vitamin B12 transporter BtuCD-F
    • Korkhov VM, Mireku SA, Locher KP (2012) Structure of AMP-PNP-bound vitamin B12 transporter BtuCD-F. Nature 490:367–372. doi:10.1038/nature11442
    • (2012) Nature , vol.490 , pp. 367-372
    • Korkhov, V.M.1    Mireku, S.A.2    Locher, K.P.3
  • 76
    • 84876665028 scopus 로고    scopus 로고
    • Fate of ferrisiderophores after import across bacterial outer membranes: Different iron release strategies are observed in the cytoplasm or periplasm depending on the siderophore pathways
    • Schalk IJ, Guillon L (2013) Fate of ferrisiderophores after import across bacterial outer membranes: different iron release strategies are observed in the cytoplasm or periplasm depending on the siderophore pathways. Amino Acids 44:1267–1277. doi:10.1007/s00726-013-1468-2
    • (2013) Amino Acids , vol.44 , pp. 1267-1277
    • Schalk, I.J.1    Guillon, L.2
  • 77
    • 84933510945 scopus 로고    scopus 로고
    • Structure and mechanism of the siderophore-interacting protein from the fuscachelin gene cluster of Thermobifida fusca
    • Li K, Chen W-H, Bruner SD (2015) Structure and mechanism of the siderophore-interacting protein from the fuscachelin gene cluster of Thermobifida fusca. Biochemistry 54:3989–4000. doi:10.1021/acs.biochem.5b00354
    • (2015) Biochemistry , vol.54 , pp. 3989-4000
    • Li, K.1    Chen, W.-H.2    Bruner, S.D.3
  • 78
    • 23744479843 scopus 로고    scopus 로고
    • In vitro characterization of salmochelin and enterobactin trilactone hydrolases IroD, IroE, and Fes
    • Lin H, Fischbach MA, Liu DR, Walsh CT (2005) In vitro characterization of salmochelin and enterobactin trilactone hydrolases IroD, IroE, and Fes. J Am Chem Soc 127:11075–11084. doi:10.1021/ja0522027
    • (2005) J am Chem Soc , vol.127 , pp. 11075-11084
    • Lin, H.1    Fischbach, M.A.2    Liu, D.R.3    Walsh, C.T.4
  • 79
    • 0028467772 scopus 로고
    • Structure of a unique twofold symmetric haem-binding site
    • Frolow F, Kalb AJ, Yariv J (1994) Structure of a unique twofold symmetric haem-binding site. Nat Struct Biol 1:453–460. doi:10.1038/nsb0794-453
    • (1994) Nat Struct Biol , vol.1 , pp. 453-460
    • Frolow, F.1    Kalb, A.J.2    Yariv, J.3
  • 80
    • 84937780279 scopus 로고    scopus 로고
    • Recent developments in understanding the iron acquisition strategies of gram positive pathogens
    • Sheldon JR, Heinrichs DE (2015) Recent developments in understanding the iron acquisition strategies of gram positive pathogens. FEMS Microbiol Rev 39:592–630. doi:10.1093/femsre/fuv009
    • (2015) FEMS Microbiol Rev , vol.39 , pp. 592-630
    • Sheldon, J.R.1    Heinrichs, D.E.2
  • 81
    • 0034718606 scopus 로고    scopus 로고
    • Microbial iron transport via a siderophore shuttle: A membrane ion transport paradigm
    • Stintzi A, Barnes C, Xu J, Raymond KN (2000) Microbial iron transport via a siderophore shuttle: a membrane ion transport paradigm. Proc Natl Acad Sci U S A 97:10691–10696. doi:10.1073/pnas.200318797
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 10691-10696
    • Stintzi, A.1    Barnes, C.2    Xu, J.3    Raymond, K.N.4
  • 82
    • 84882747810 scopus 로고    scopus 로고
    • Gram-positive siderophore-shuttle with iron-exchange from Fe-siderophore to apo-siderophore by Bacillus cereus YxeB
    • Fukushima T, Allred BE, Sia AK, Nichiporuk R, Andersen UN, Raymond KN (2013) Gram-positive siderophore-shuttle with iron-exchange from Fe-siderophore to apo-siderophore by Bacillus cereus YxeB. Proc Natl Acad Sci U S A 110:13821–13826. doi:10.1073/pnas. 1304235110
    • (2013) Proc Natl Acad Sci U S A , vol.110 , pp. 13821-13826
    • Fukushima, T.1    Allred, B.E.2    Sia, A.K.3    Nichiporuk, R.4    Andersen, U.N.5    Raymond, K.N.6
  • 83
    • 84913600844 scopus 로고    scopus 로고
    • Direct evidence of iron uptake by the Gram-positive siderophore-shuttle mechanism without iron reduction
    • Fukushima T, Allred BE, Raymond KN (2014) Direct evidence of iron uptake by the Gram-positive siderophore-shuttle mechanism without iron reduction. ACS Chem Biol 9:2092–2100. doi:10.1021/cb500319n
    • (2014) ACS Chem Biol , vol.9 , pp. 2092-2100
    • Fukushima, T.1    Allred, B.E.2    Raymond, K.N.3
  • 85
    • 35448937302 scopus 로고
    • Mechanism of action of sideromycins
    • Knusel F, Nuesch J (1965) Mechanism of action of sideromycins. Nature 206:674–676. doi:10.1038/206674a0
    • (1965) Nature , vol.206 , pp. 674-676
    • Knusel, F.1    Nuesch, J.2
  • 86
    • 33744744409 scopus 로고    scopus 로고
    • Albomycin uptake via a ferric hydroxamate transport system of Streptococcus pneumoniae R6
    • Pramanik A, Braun V (2006) Albomycin uptake via a ferric hydroxamate transport system of Streptococcus pneumoniae R6. J Bacteriol 188:3878–3886. doi:10.1128/jb.00205-06
    • (2006) J Bacteriol , vol.188 , pp. 3878-3886
    • Pramanik, A.1    Braun, V.2
  • 87
    • 33744725409 scopus 로고
    • Recent studies on albomycin, a new antibiotic
    • doi:10. 1136/bmj.2.4949.1177
    • Gause GF (1955) Recent studies on albomycin, a new antibiotic. BMJ 2:1177–1179. doi:10. 1136/bmj.2.4949.1177
    • (1955) BMJ , vol.2 , pp. 1177-1179
    • Gause, G.F.1
  • 88
    • 84868087343 scopus 로고    scopus 로고
    • Biosynthesis of albomycin δ(2) provides a template for assembling siderophore and aminoacyl-tRNA synthetase inhibitor conjugates
    • Zeng Y, Kulkarni A, Yang Z, Patil PB, Zhou W, Chi X, Van Lanen S, Chen S (2012) Biosynthesis of albomycin δ(2) provides a template for assembling siderophore and aminoacyl-tRNA synthetase inhibitor conjugates. ACS Chem Biol 7:1565–1575. doi:10. 1021/cb300173x
    • (2012) ACS Chem Biol , vol.7 , pp. 1565-1575
    • Zeng, Y.1    Kulkarni, A.2    Yang, Z.3    Patil, P.B.4    Zhou, W.5    Chi, X.6    van Lanen, S.7    Chen, S.8
  • 89
    • 84953896573 scopus 로고    scopus 로고
    • A branch point of Streptomyces sulfur amino acid metabolism controls the production of albomycin
    • Kulkarni A, Zeng Y, Zhou W, Van Lanen S, Zhang W, Chen S (2015) A branch point of Streptomyces sulfur amino acid metabolism controls the production of albomycin. Appl Environ Microbiol 82:467–477. doi:10.1128/aem.02517-15
    • (2015) Appl Environ Microbiol , vol.82 , pp. 467-477
    • Kulkarni, A.1    Zeng, Y.2    Zhou, W.3    van Lanen, S.4    Zhang, W.5    Chen, S.6
  • 90
    • 0034525966 scopus 로고    scopus 로고
    • A potent seryl tRNA synthetase inhibitor SB-217452 isolated from a Streptomyces species
    • Stefanska AL, Fulston M, Houge-Frydrych CS, Jones JJ, Warr SR (2000) A potent seryl tRNA synthetase inhibitor SB-217452 isolated from a Streptomyces species. J Antibiot 53:1346–1353. doi:10.7164/antibiotics.53.1346
    • (2000) J Antibiot , vol.53 , pp. 1346-1353
    • Stefanska, A.L.1    Fulston, M.2    Houge-Frydrych, C.S.3    Jones, J.J.4    Warr, S.R.5
  • 91
    • 70350307194 scopus 로고    scopus 로고
    • Characterization of two seryl-tRNA synthetases in albomycin-producing Streptomyces sp. Strain ATCC 700974
    • Zeng Y, Roy H, Patil PB, Ibba M, Chen S (2009) Characterization of two seryl-tRNA synthetases in albomycin-producing Streptomyces sp. strain ATCC 700974. Antimicrob Agents Chemother 53:4619–4627. doi:10.1128/aac.00782-09
    • (2009) Antimicrob Agents Chemother , vol.53 , pp. 4619-4627
    • Zeng, Y.1    Roy, H.2    Patil, P.B.3    Ibba, M.4    Chen, S.5
  • 92
    • 0034079929 scopus 로고    scopus 로고
    • Crystal structure of the antibiotic albomycin in complex with the outer membrane transporter FhuA
    • Ferguson AD, Braun V, Fiedler HP, Coulton JW, Diederichs K, Welte W (2000) Crystal structure of the antibiotic albomycin in complex with the outer membrane transporter FhuA. Protein Sci 9:956–963. doi:10.1110/ps.9.5.956
    • (2000) Protein Sci , vol.9 , pp. 956-963
    • Ferguson, A.D.1    Braun, V.2    Fiedler, H.P.3    Coulton, J.W.4    Diederichs, K.5    Welte, W.6
  • 93
    • 0037134502 scopus 로고    scopus 로고
    • X-ray crystallographic structures of the Escherichia coli periplasmic protein FhuD bound to hydroxamate-type siderophores and the antibiotic albomycin
    • Clarke TE, Braun V, Winkelmann G, Tari LW, Vogel HJ (2002) X-ray crystallographic structures of the Escherichia coli periplasmic protein FhuD bound to hydroxamate-type siderophores and the antibiotic albomycin. J Biol Chem 277:13966–13972. doi:10.1074/jbc.M109385200
    • (2002) J Biol Chem , vol.277 , pp. 13966-13972
    • Clarke, T.E.1    Braun, V.2    Winkelmann, G.3    Tari, L.W.4    Vogel, H.J.5
  • 94
    • 0020627683 scopus 로고
    • Intracellular activation of albomycin in Escherichia coli and Salmonella typhimurium
    • Braun V, Gunthner K, Hantke K, Zimmermann L (1983) Intracellular activation of albomycin in Escherichia coli and Salmonella typhimurium. J Bacteriol 156:308–315
    • (1983) J Bacteriol , vol.156 , pp. 308-315
    • Braun, V.1    Gunthner, K.2    Hantke, K.3    Zimmermann, L.4
  • 96
    • 0029094662 scopus 로고
    • Salmycin A–D, antibiotika aus Streptomyces violaceus, DSM 8286, mit siderophor-aminoglycosid-struktur
    • Vértesy L, Aretz W, Fehlhaber H-W, Kogler H (1995) Salmycin A–D, antibiotika aus Streptomyces violaceus, DSM 8286, mit siderophor-aminoglycosid-struktur. Helv Chim Acta 78:46–60. doi:10.1002/hlca.19950780105
    • (1995) Helv Chim Acta , vol.78 , pp. 46-60
    • Vértesy, L.1    Aretz, W.2    Fehlhaber, H.-W.3    Kogler, H.4
  • 97
    • 0022632136 scopus 로고
    • Stoffwechselprodukte von mikroorganismen. 233. Mitteilung. Danoxamin, der eisenbindende teil des sideromycin-antibioticums danomycin
    • Huber P, Leuenberger H, Keller-Schierlein W (1986) Stoffwechselprodukte von mikroorganismen. 233. Mitteilung. Danoxamin, der eisenbindende teil des sideromycin-antibioticums danomycin. Helv Chim Acta 69:236–245. doi:10.1002/hlca.19860690128
    • (1986) Helv Chim Acta , vol.69 , pp. 236-245
    • Huber, P.1    Leuenberger, H.2    Keller-Schierlein, W.3
  • 99
    • 67651247598 scopus 로고    scopus 로고
    • Is drug release necessary for antimicrobial activity of siderophore-drug conjugates? Syntheses and biological studies of the naturally occurring salmycin “Trojan horse” antibiotics and synthetic desferridanoxamine-antibiotic conjugates
    • Wencewicz TA, M€ollmann U, Long TE, Miller MJ (2009) Is drug release necessary for antimicrobial activity of siderophore-drug conjugates? Syntheses and biological studies of the naturally occurring salmycin “Trojan horse” antibiotics and synthetic desferridanoxamine-antibiotic conjugates. Biometals 22:633–648. doi:10.1007/s10534-009-9218-3
    • (2009) Biometals , vol.22 , pp. 633-648
    • Wencewicz, T.A.1    M€Ollmann, U.2    Long, T.E.3    Miller, M.J.4
  • 100
    • 33747074333 scopus 로고    scopus 로고
    • Identification of genes involved in siderophore transport in Streptomyces coelicolor A3(2)
    • Bunet R, Brock A, Rexer HU, Takano E (2006) Identification of genes involved in siderophore transport in Streptomyces coelicolor A3(2). FEMS Microbiol Lett 262:57–64. doi:10.1111/j.1574-6968.2006.00362.x
    • (2006) FEMS Microbiol Lett , vol.262 , pp. 57-64
    • Bunet, R.1    Brock, A.2    Rexer, H.U.3    Takano, E.4
  • 103
    • 84919467117 scopus 로고    scopus 로고
    • Deferoxamine mesylate enhances virulence of community-associated methicillin resistant Staphylococcus aureus
    • Arifin AJ, Hannauer M, Welch I, Heinrichs DE (2014) Deferoxamine mesylate enhances virulence of community-associated methicillin resistant Staphylococcus aureus. Microbes Infect 16:967–972. doi:10.1016/j.micinf.2014.09.003
    • (2014) Microbes Infect , vol.16 , pp. 967-972
    • Arifin, A.J.1    Hannauer, M.2    Welch, I.3    Heinrichs, D.E.4
  • 104
    • 21044449406 scopus 로고    scopus 로고
    • A widely distributed bacterial pathway for siderophore biosynthesis independent of nonribosomal peptide synthetases
    • Challis GL (2005) A widely distributed bacterial pathway for siderophore biosynthesis independent of nonribosomal peptide synthetases. ChemBioChem 6:601–611. doi:10.1002/cbic.200400283
    • (2005) Chembiochem , vol.6 , pp. 601-611
    • Challis, G.L.1
  • 105
    • 0034637519 scopus 로고    scopus 로고
    • Total synthesis of the siderophore danoxamine
    • Roosenberg II JM, Miller MJ (2000) Total synthesis of the siderophore danoxamine. J Org Chem 65:4833–4838. doi:10.1021/jo000050m
    • (2000) J Org Chem , vol.65 , pp. 4833-4838
    • Roosenberg, J.M.1    Miller, M.J.2
  • 106
    • 0037132597 scopus 로고    scopus 로고
    • Total synthesis of desferrisalmycin B
    • Dong L, Roosenberg II JM, Miller MJ (2002) Total synthesis of desferrisalmycin B. J Am Chem Soc 124(50):15001–15005. doi:10.1021/ja028386w
    • (2002) J am Chem Soc , vol.124 , Issue.50 , pp. 15001-15005
    • Dong, L.1    Roosenberg, J.M.2    Miller, M.J.3
  • 107
    • 34250968659 scopus 로고
    • Metabolites of actinomycetes. 28. “In vitro” resistance to ferrimycin
    • Bachmann E, Zaehner H (1961) Metabolites of actinomycetes. 28. “In vitro” resistance to ferrimycin. Arch Mikrobiol 38:326–338
    • (1961) Arch Mikrobiol , vol.38 , pp. 326-338
    • Bachmann, E.1    Zaehner, H.2
  • 109
    • 3242836200 scopus 로고
    • Stoffwechselprodukte von mikroorganismen – 53: Ueber die konstitution von ferrimycin A1
    • Bickel H, Mertens P, Prelog V, Seibl J, Walser A (1966) Stoffwechselprodukte von mikroorganismen – 53: ueber die konstitution von ferrimycin A1. Tetrahedron 22:171–179. doi:10.1016/S0040-4020(01)82182-7
    • (1966) Tetrahedron , vol.22 , pp. 171-179
    • Bickel, H.1    Mertens, P.2    Prelog, V.3    Seibl, J.4    Walser, A.5
  • 111
    • 0025157461 scopus 로고
    • Ferrioxamine transport mutants and the identification of the ferrioxamine receptor protein (FoxA) in Erwinia herbicola (Enterobacter agglomerans)
    • Berner I, Winkelmann G (1990) Ferrioxamine transport mutants and the identification of the ferrioxamine receptor protein (FoxA) in Erwinia herbicola (Enterobacter agglomerans). Biol Met 2:197–202. doi:10.1007/BF01141359
    • (1990) Biol Met , vol.2 , pp. 197-202
    • Berner, I.1    Winkelmann, G.2
  • 114
    • 34447528296 scopus 로고    scopus 로고
    • Microcins, gene-encoded antibacterial peptides from enterobacteria
    • Duquesne S, Destoumieux-Garzon D, Peduzzi J, Rebuffat S (2007) Microcins, gene-encoded antibacterial peptides from enterobacteria. Nat Prod Rep 24:708–734. doi:10.1039/b516237h
    • (2007) Nat Prod Rep , vol.24 , pp. 708-734
    • Duquesne, S.1    Destoumieux-Garzon, D.2    Peduzzi, J.3    Rebuffat, S.4
  • 116
    • 36448952357 scopus 로고    scopus 로고
    • Biosynthetic tailoring of microcin E492m: Post-translational modification affords an antibacterial siderophore peptide conjugate
    • Nolan EM, Fischbach MA, Koglin A, Walsh CT (2007) Biosynthetic tailoring of microcin E492m: post-translational modification affords an antibacterial siderophore peptide conjugate. J Am Chem Soc 129:14336–14347. doi:10.1021/ja074650f
    • (2007) J am Chem Soc , vol.129 , pp. 14336-14347
    • Nolan, E.M.1    Fischbach, M.A.2    Koglin, A.3    Walsh, C.T.4
  • 117
    • 50849105102 scopus 로고    scopus 로고
    • Investigations of the MceIJ-catalyzed posttranslational modification of the microcin E492 C-terminus: Linkage of ribosomal and nonribosomal peptides to form “Trojan horse” antibiotics
    • Nolan EM, Walsh CT (2008) Investigations of the MceIJ-catalyzed posttranslational modification of the microcin E492 C-terminus: linkage of ribosomal and nonribosomal peptides to form “Trojan horse” antibiotics. Biochemistry 47:9289–9299. doi:10.1021/bi800826j
    • (2008) Biochemistry , vol.47 , pp. 9289-9299
    • Nolan, E.M.1    Walsh, C.T.2
  • 118
    • 84878324193 scopus 로고    scopus 로고
    • Tetroazolemycins A and B, two new oxazole-thiazole siderophores from deep-sea Streptomyces olivaceus FXJ8.012
    • Liu N, Shang F, Xi L, Huang Y (2013) Tetroazolemycins A and B, two new oxazole-thiazole siderophores from deep-sea Streptomyces olivaceus FXJ8.012. Mar Drugs 11:1524–1533. doi:10.3390/md11051524
    • (2013) Mar Drugs , vol.11 , pp. 1524-1533
    • Liu, N.1    Shang, F.2    Xi, L.3    Huang, Y.4
  • 119
    • 79961121513 scopus 로고    scopus 로고
    • Klebsiella pneumoniae yersiniabactin promotes respiratory tract infection through evasion of lipocalin 2
    • Bachman MA, Oyler JE, Burns SH, Caza M, Lepine F, Dozois CM, Weiser JN (2011) Klebsiella pneumoniae yersiniabactin promotes respiratory tract infection through evasion of lipocalin 2. Infect Immun 79:3309–3316. doi:10.1128/iai.05114-11
    • (2011) Infect Immun , vol.79 , pp. 3309-3316
    • Bachman, M.A.1    Oyler, J.E.2    Burns, S.H.3    Caza, M.4    Lepine, F.5    Dozois, C.M.6    Weiser, J.N.7
  • 120
    • 84857527566 scopus 로고    scopus 로고
    • Pyochelin, a siderophore of Pseudomonas aeruginosa: Physicochemical characterization of the iron(iii), copper(ii) and zinc(ii) complexes
    • Brandel J, Humbert N, Elhabiri M, Schalk IJ, Mislin GLA, Albrecht-Gary A-M (2012) Pyochelin, a siderophore of Pseudomonas aeruginosa: physicochemical characterization of the iron(iii), copper(ii) and zinc(ii) complexes. Dalton Trans 41:2820–2834. doi:10.1039/C1DT11804H
    • (2012) Dalton Trans , vol.41 , pp. 2820-2834
    • Brandel, J.1    Humbert, N.2    Elhabiri, M.3    Schalk, I.J.4    Mislin, G.L.A.5    Albrecht-Gary, A.-M.6
  • 123
    • 84872850695 scopus 로고    scopus 로고
    • Siderophore conjugates
    • Page MG (2013) Siderophore conjugates. Ann N Y Acad Sci 1277:115–126. doi:10.1111/nyas.12024
    • (2013) Ann N Y Acad Sci , vol.1277 , pp. 115-126
    • Page, M.G.1
  • 124
    • 84863393586 scopus 로고    scopus 로고
    • Exploiting bacterial iron acquisition: Siderophore conjugates
    • Ji C, Juarez-Hernandez RE, Miller MJ (2012) Exploiting bacterial iron acquisition: siderophore conjugates. Future Med Chem 4:297–313. doi:10.4155/fmc.11.191
    • (2012) Future Med Chem , vol.4 , pp. 297-313
    • Ji, C.1    Juarez-Hernandez, R.E.2    Miller, M.J.3
  • 125
    • 84905299821 scopus 로고    scopus 로고
    • Siderophore–drug complexes: Potential medicinal applications of the ‘Trojan horse’ strategy
    • Górska A, Sloderbach A, Marszałł MP (2014) Siderophore–drug complexes: potential medicinal applications of the ‘Trojan horse’ strategy. Trends Pharmacol Sci 35:442–449. doi:10.1016/j.tips.2014.06.007
    • (2014) Trends Pharmacol Sci , vol.35 , pp. 442-449
    • Górska, A.1    Sloderbach, A.2    Marszałł, M.P.3
  • 126
    • 84896879592 scopus 로고    scopus 로고
    • Siderophore-dependent iron uptake systems as gates for antibiotic Trojan horse strategies against Pseudomonas aeruginosa
    • Mislin GL, Schalk IJ (2014) Siderophore-dependent iron uptake systems as gates for antibiotic Trojan horse strategies against Pseudomonas aeruginosa. Metallomics 6:408–420. doi:10.1039/c3mt00359k
    • (2014) Metallomics , vol.6 , pp. 408-420
    • Mislin, G.L.1    Schalk, I.J.2
  • 127
    • 84965014151 scopus 로고    scopus 로고
    • Microbial siderophore-based iron assimilation and therapeutic applications
    • Li K, Chen W-H, Bruner SD (2016) Microbial siderophore-based iron assimilation and therapeutic applications. Biometals 29:377–388. doi:10.1007/s10534-016-9935-3
    • (2016) Biometals , vol.29 , pp. 377-388
    • Li, K.1    Chen, W.-H.2    Bruner, S.D.3
  • 128
    • 85017495826 scopus 로고    scopus 로고
    • Trojan horse antibiotics – a novel way to circumvent gram-negative bacterial resistance?
    • Tillotson GS (2016) Trojan horse antibiotics – a novel way to circumvent gram-negative bacterial resistance? Infect Dis 9:45–52. doi:10.4137/idrt.s31567
    • (2016) Infect Dis , vol.9 , pp. 45-52
    • Tillotson, G.S.1
  • 129
    • 85008311832 scopus 로고    scopus 로고
    • Design, synthesis and microbiological evaluation of ampicillin-tetramic acid hybrid antibiotics
    • Cherian PT, Deshpande A, Cheramie MN, Bruhn DF, Hurdle JG, Lee RE (2017) Design, synthesis and microbiological evaluation of ampicillin-tetramic acid hybrid antibiotics. J Antibiot 70:65–72. doi:10.1038/ja.2016.52
    • (2017) J Antibiot , vol.70 , pp. 65-72
    • Cherian, P.T.1    Deshpande, A.2    Cheramie, M.N.3    Bruhn, D.F.4    Hurdle, J.G.5    Lee, R.E.6
  • 131
    • 9744232909 scopus 로고    scopus 로고
    • Time-related differences in the physical property profiles of oral drugs
    • Leeson PD, Davis AM (2004) Time-related differences in the physical property profiles of oral drugs. J Med Chem 47:6338–6348. https://doi.org/10.1021/jm049717d
    • (2004) J Med Chem , vol.47 , pp. 6338-6348
    • Leeson, P.D.1    Davis, A.M.2
  • 132
    • 0031684186 scopus 로고    scopus 로고
    • Synthesis and in vitro antibacterial activity of catechol-spiramycin conjugates
    • Poras H, Kunesch G, Barriere JC, Berthaud N, Andremont A (1998) Synthesis and in vitro antibacterial activity of catechol-spiramycin conjugates. J Antibiot 51:786–794. doi:10.7164/antibiotics.51.786
    • (1998) J Antibiot , vol.51 , pp. 786-794
    • Poras, H.1    Kunesch, G.2    Barriere, J.C.3    Berthaud, N.4    Andremont, A.5
  • 133
    • 0028793908 scopus 로고
    • Design, synthesis, and biological evaluation of isocyanurate-based antifungal and macrolide antibiotic conjugates: Iron transport-mediated drug delivery
    • Ghosh M, Miller MJ (1995) Design, synthesis, and biological evaluation of isocyanurate-based antifungal and macrolide antibiotic conjugates: iron transport-mediated drug delivery. Bioorg Med Chem 3:1519–1525. doi:10.1016/0968-0896(95)00134-3
    • (1995) Bioorg Med Chem , vol.3 , pp. 1519-1525
    • Ghosh, M.1    Miller, M.J.2
  • 134
    • 79953034977 scopus 로고    scopus 로고
    • An artificial pathway to 3,4-dihydroxybenzoic acid allows generation of new aminocoumarin antibiotic recognized by catechol transporters of E. Coli
    • Alt S, Burkard N, Kulik A, Grond S, Heide L (2011) An artificial pathway to 3,4-dihydroxybenzoic acid allows generation of new aminocoumarin antibiotic recognized by catechol transporters of E. coli. Chem Biol 18:304–313. doi:10.1016/j.chembiol.2010.12.016
    • (2011) Chem Biol , vol.18 , pp. 304-313
    • Alt, S.1    Burkard, N.2    Kulik, A.3    Grond, S.4    Heide, L.5
  • 135
    • 11244258728 scopus 로고    scopus 로고
    • Desketoneoenactin-siderophore conjugates for Candida: Evidence of iron transport-dependent species selectivity
    • Bernier G, Girijavallabhan V, Murray A, Niyaz N, Ding P, Miller MJ, Malouin F (2005) Desketoneoenactin-siderophore conjugates for Candida: evidence of iron transport-dependent species selectivity. Antimicrob Agents Chemother 49:241–248. doi:10.1128/aac. 49.1.241-248.2005
    • (2005) Antimicrob Agents Chemother , vol.49 , pp. 241-248
    • Bernier, G.1    Girijavallabhan, V.2    Murray, A.3    Niyaz, N.4    Ding, P.5    Miller, M.J.6    Malouin, F.7
  • 136
    • 0033384172 scopus 로고    scopus 로고
    • Syntheses and studies of multiwarhead siderophore-5-fluorouridine conjugates
    • Lu Y, Miller MJ (1999) Syntheses and studies of multiwarhead siderophore-5-fluorouridine conjugates. Bioorg Med Chem 7:3025–3038. doi:10.1016/S0968-0896(99)00248-5
    • (1999) Bioorg Med Chem , vol.7 , pp. 3025-3038
    • Lu, Y.1    Miller, M.J.2
  • 139
    • 0030014795 scopus 로고    scopus 로고
    • Framework-reactive siderophore analogs as potential cell-selective drugs. Design and syntheses of trimelamol-based iron chelators
    • Ramurthy S, Miller MJ (1996) Framework-reactive siderophore analogs as potential cell-selective drugs. Design and syntheses of trimelamol-based iron chelators. J Org Chem 61:4120–4124. doi:10.1021/jo9600621
    • (1996) J Org Chem , vol.61 , pp. 4120-4124
    • Ramurthy, S.1    Miller, M.J.2
  • 140
    • 84867393274 scopus 로고    scopus 로고
    • Syntheses of siderophore–drug conjugates using a convergent thiol–maleimide system
    • doi:10. 1021/ml300150y
    • Juárez-Hernández RE, Miller PA, Miller MJ (2012) Syntheses of siderophore–drug conjugates using a convergent thiol–maleimide system. ACS Med Chem Lett 3:799–803. doi:10. 1021/ml300150y
    • (2012) ACS Med Chem Lett , vol.3 , pp. 799-803
    • Juárez-Hernández, R.E.1    Miller, P.A.2    Miller, M.J.3
  • 141
    • 0029962175 scopus 로고    scopus 로고
    • Synthesis and in vitro antibacterial activity of spermidine-based mixed catechol-and hydroxamate-containing siderophore–vancomycin conjugates
    • Ghosh M, Miller MJ (1996) Synthesis and in vitro antibacterial activity of spermidine-based mixed catechol-and hydroxamate-containing siderophore–vancomycin conjugates. Bioorg Med Chem 4:43–48. doi:10.1016/0968-0896(95)00161-1
    • (1996) Bioorg Med Chem , vol.4 , pp. 43-48
    • Ghosh, M.1    Miller, M.J.2
  • 142
    • 79952773032 scopus 로고    scopus 로고
    • Chemical synthesis and biological evaluation of gallidermin-siderophore conjugates
    • Yoganathan S, Sit CS, Vederas JC (2011) Chemical synthesis and biological evaluation of gallidermin-siderophore conjugates. Org Biomol Chem 9:2133–2141. doi:10.1039/c0ob00846j
    • (2011) Org Biomol Chem , vol.9 , pp. 2133-2141
    • Yoganathan, S.1    Sit, C.S.2    Vederas, J.C.3
  • 143
    • 85020376124 scopus 로고    scopus 로고
    • Targeted antibiotic delivery: Selective siderophore conjugation with daptomycin confers potent activity against multidrug resistant Acinetobacter baumannii both in vitro and in vivo
    • Epub ahead of print
    • Ghosh M, Miller PA, M€ollmann U, Claypool WD, Schroeder VA, Wolter WR, Suckow M, Yu H, Li S, Huang W, Zajicek J, Miller MJ (2017) Targeted antibiotic delivery: selective siderophore conjugation with daptomycin confers potent activity against multidrug resistant Acinetobacter baumannii both in vitro and in vivo. J Med Chem. doi:10.1021/acs.jmedchem. 7b00102 (Epub ahead of print)
    • (2017) J Med Chem
    • Ghosh, M.1    Miller, P.A.2    M€Ollmann, U.3    Claypool, W.D.4    Schroeder, V.A.5    Wolter, W.R.6    Suckow, M.7    Yu, H.8    Li, S.9    Huang, W.10    Zajicek, J.11    Miller, M.J.12
  • 145
    • 0025172945 scopus 로고
    • Synthesis and structure-activity relationships of monocarbams leading to U-78608
    • Barbachyn MR, Tuominen TC (1990) Synthesis and structure-activity relationships of monocarbams leading to U-78608. J Antibiot 43:1199–1203. doi:10.7164/antibiotics.43.1199
    • (1990) J Antibiot , vol.43 , pp. 1199-1203
    • Barbachyn, M.R.1    Tuominen, T.C.2
  • 146
    • 84859602519 scopus 로고    scopus 로고
    • In vitro activity of the siderophore monosulfactam BAL30072 against meropenem-non-susceptible Acinetobacter baumannii
    • Higgins PG, Stefanik D, Page MG, Hackel M, Seifert H (2012) In vitro activity of the siderophore monosulfactam BAL30072 against meropenem-non-susceptible Acinetobacter baumannii. J Antimicrob Chemother 67:1167–1169. doi:10.1093/jac/dks009
    • (2012) J Antimicrob Chemother , vol.67 , pp. 1167-1169
    • Higgins, P.G.1    Stefanik, D.2    Page, M.G.3    Hackel, M.4    Seifert, H.5
  • 147
    • 84877127230 scopus 로고    scopus 로고
    • Combined effects of the siderophore monosulfactam BAL30072 and carbapenems on multidrug-resistant Gram-negative bacilli
    • Hofer B, Dantier C, Gebhardt K, Desarbre E, Schmitt-Hoffmann A, Page MG (2013) Combined effects of the siderophore monosulfactam BAL30072 and carbapenems on multidrug-resistant Gram-negative bacilli. J Antimicrob Chemother 68:1120–1129. doi:10. 1093/jac/dks527
    • (2013) J Antimicrob Chemother , vol.68 , pp. 1120-1129
    • Hofer, B.1    Dantier, C.2    Gebhardt, K.3    Desarbre, E.4    Schmitt-Hoffmann, A.5    Page, M.G.6
  • 148
    • 84884700230 scopus 로고    scopus 로고
    • In vitro activity of the novel monosulfactam BAL30072 alone and in combination with meropenem versus a diverse collection of important Gram-negative pathogens
    • Hornsey M, Phee L, Stubbings W, Wareham DW (2013) In vitro activity of the novel monosulfactam BAL30072 alone and in combination with meropenem versus a diverse collection of important Gram-negative pathogens. Int J Antimicrob Agents 42:343–346. doi:10.1016/j.ijantimicag.2013.05.010
    • (2013) Int J Antimicrob Agents , vol.42 , pp. 343-346
    • Hornsey, M.1    Phee, L.2    Stubbings, W.3    Wareham, D.W.4
  • 149
    • 84902082853 scopus 로고    scopus 로고
    • In vitro activity of the siderophore monosulfactam BAL30072 against contemporary Gram-negative pathogens from New York City, including multidrug-resistant isolates
    • Landman D, Singh M, El-Imad B, Miller E, Win T, Quale J (2014) In vitro activity of the siderophore monosulfactam BAL30072 against contemporary Gram-negative pathogens from New York City, including multidrug-resistant isolates. Int J Antimicrob Agents 43:527–532. doi:10.1016/j.ijantimicag.2014.02.017
    • (2014) Int J Antimicrob Agents , vol.43 , pp. 527-532
    • Landman, D.1    Singh, M.2    El-Imad, B.3    Miller, E.4    Win, T.5    Quale, J.6
  • 150
    • 77950215859 scopus 로고    scopus 로고
    • Activity of the siderophore monobactam BAL30072 against multiresistant non-fermenters
    • Mushtaq S, Warner M, Livermore D (2010) Activity of the siderophore monobactam BAL30072 against multiresistant non-fermenters. J Antimicrob Chemother 65:266–270. doi:10.1093/jac/dkp425
    • (2010) J Antimicrob Chemother , vol.65 , pp. 266-270
    • Mushtaq, S.1    Warner, M.2    Livermore, D.3
  • 151
    • 77952614275 scopus 로고    scopus 로고
    • In vitro properties of BAL30072, a novel siderophore sulfactam with activity against multiresistant gram-negative bacilli
    • Page MG, Dantier C, Desarbre E (2010) In vitro properties of BAL30072, a novel siderophore sulfactam with activity against multiresistant gram-negative bacilli. Antimicrob Agents Chemother 54:2291–2302. doi:10.1128/aac.01525-09
    • (2010) Antimicrob Agents Chemother , vol.54 , pp. 2291-2302
    • Page, M.G.1    Dantier, C.2    Desarbre, E.3
  • 153
    • 84876213849 scopus 로고    scopus 로고
    • Involvement of Fe uptake systems and AmpC beta-lactamase in susceptibility to the siderophore monosulfactam BAL30072 in Pseudomonas aeruginosa
    • van Delden C, Page MG, Kohler T (2013) Involvement of Fe uptake systems and AmpC beta-lactamase in susceptibility to the siderophore monosulfactam BAL30072 in Pseudomonas aeruginosa. Antimicrob Agents Chemother 57:2095–2102. doi:10.1128/aac.02474-12
    • (2013) Antimicrob Agents Chemother , vol.57 , pp. 2095-2102
    • van Delden, C.1    Page, M.G.2    Kohler, T.3
  • 155
    • 78650656571 scopus 로고    scopus 로고
    • Structural basis for effectiveness of siderophore-conjugated monocarbams against clinically relevant strains of Pseudomonas aeruginosa
    • Han S, Zaniewski RP, Marr ES, Lacey BM, Tomaras AP, Evdokimov A, Miller JR, Shanmugasundaram V (2010) Structural basis for effectiveness of siderophore-conjugated monocarbams against clinically relevant strains of Pseudomonas aeruginosa. Proc Natl Acad Sci U S A 107:22002–22007. doi:10.1073/pnas.1013092107
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 22002-22007
    • Han, S.1    Zaniewski, R.P.2    Marr, E.S.3    Lacey, B.M.4    Tomaras, A.P.5    Evdokimov, A.6    Miller, J.R.7    Shanmugasundaram, V.8
  • 157
    • 84996478385 scopus 로고    scopus 로고
    • Siderophore cephalosporin cefiderocol utilizes ferric iron transporter systems for antibacterial activity against Pseudomonas aeruginosa
    • Ito A, Nishikawa T, Matsumoto S, Yoshizawa H, Sato T, Nakamura R, Tsuji M, Yamano Y (2016) Siderophore cephalosporin cefiderocol utilizes ferric iron transporter systems for antibacterial activity against Pseudomonas aeruginosa. Antimicrob Agents Chemother 60:7396–7401. doi:10.1128/aac.01405-16
    • (2016) Antimicrob Agents Chemother , vol.60 , pp. 7396-7401
    • Ito, A.1    Nishikawa, T.2    Matsumoto, S.3    Yoshizawa, H.4    Sato, T.5    Nakamura, R.6    Tsuji, M.7    Yamano, Y.8
  • 159
    • 84957895337 scopus 로고    scopus 로고
    • In vitro antimicrobial activity of a siderophore cephalosporin, S-649266, against Enterobacteriaceae clinical isolates, including carbapenem-resistant strains
    • Kohira N, West J, Ito A, Ito-Horiyama T, Nakamura R, Sato T, Rittenhouse S, Tsuji M, Yamano Y (2016) In vitro antimicrobial activity of a siderophore cephalosporin, S-649266, against Enterobacteriaceae clinical isolates, including carbapenem-resistant strains. Antimicrob Agents Chemother 60:729–734. doi:10.1128/aac.01695-15
    • (2016) Antimicrob Agents Chemother , vol.60 , pp. 729-734
    • Kohira, N.1    West, J.2    Ito, A.3    Ito-Horiyama, T.4    Nakamura, R.5    Sato, T.6    Rittenhouse, S.7    Tsuji, M.8    Yamano, Y.9
  • 160
    • 9744232909 scopus 로고    scopus 로고
    • Time-related differences in the physical property profiles of oral drugs
    • Leeson PD, Davis AM (2004) Time-related differences in the physical property profiles of oral drugs. J Med Chem 47:6338–6348. https://doi.org/10.1021/jm049717d
    • (2004) J Med Chem , vol.47 , pp. 6338-6348
    • Leeson, P.D.1    Davis, A.M.2
  • 163
    • 0026535375 scopus 로고
    • Iron transport-mediated antibacterial activity of and development of resistance to hydroxamate and catechol siderophore-carbacepholosporin conjugates
    • Minnick AA, McKee JA, Dolence EK, Miller MJ (1992) Iron transport-mediated antibacterial activity of and development of resistance to hydroxamate and catechol siderophore-carbacepholosporin conjugates. Antimicrob Agents Chemother 36:840–850. doi:10.1128/AAC.36.4.840
    • (1992) Antimicrob Agents Chemother , vol.36 , pp. 840-850
    • Minnick, A.A.1    McKee, J.A.2    Dolence, E.K.3    Miller, M.J.4
  • 165
    • 0030453553 scopus 로고    scopus 로고
    • Iron transport-mediated drug delivery using mixed-ligand siderophore-β-lactam conjugates
    • Ghosh A, Ghosh M, Niu C, Malouin F, M€ollmann U, Miller MJ (1996) Iron transport-mediated drug delivery using mixed-ligand siderophore-β-lactam conjugates. Chem Biol 3 (12):1011–1019. doi:10.1016/S1074-5521(96)90167-2
    • (1996) Chem Biol , vol.3 , Issue.12 , pp. 1011-1019
    • Ghosh, A.1    Ghosh, M.2    Niu, C.3    Malouin, F.4    M€Ollmann, U.5    Miller, M.J.6
  • 166
    • 84878035473 scopus 로고    scopus 로고
    • Biscatecholate-monohydroxamate mixed ligand siderophore-carbacephalosporin conjugates are selective sideromycin antibiotics that target Acinetobacter baumannii
    • Wencewicz TA, Miller MJ (2013) Biscatecholate-monohydroxamate mixed ligand siderophore-carbacephalosporin conjugates are selective sideromycin antibiotics that target Acinetobacter baumannii. J Med Chem 56:4044–4052. doi:10.1021/jm400265k
    • (2013) J Med Chem , vol.56 , pp. 4044-4052
    • Wencewicz, T.A.1    Miller, M.J.2
  • 167
    • 84874994725 scopus 로고    scopus 로고
    • Structure and biosynthesis of fimsbactins A-F, siderophores from Acinetobacter baumannii and Acinetobacter baylyi
    • Proschak A, Lubuta P, Grun P, Lohr F, Wilharm G, De Berardinis V, Bode HB (2013) Structure and biosynthesis of fimsbactins A-F, siderophores from Acinetobacter baumannii and Acinetobacter baylyi. ChemBioChem 14:633–638. doi:10.1002/cbic.201200764
    • (2013) Chembiochem , vol.14 , pp. 633-638
    • Proschak, A.1    Lubuta, P.2    Grun, P.3    Lohr, F.4    Wilharm, G.5    de Berardinis, V.6    Bode, H.B.7
  • 170
    • 84870882500 scopus 로고    scopus 로고
    • Synthesis and antibacterial activity of conjugates between norfloxacin and analogues of the siderophore vanchrobactin
    • Souto A, Montaos MA, Balado M, Osorio CR, Rodriguez J, Lemos ML, Jimenez C (2013) Synthesis and antibacterial activity of conjugates between norfloxacin and analogues of the siderophore vanchrobactin. Bioorg Med Chem 21:295–302. doi:10.1016/j.bmc.2012.10.028
    • (2013) Bioorg Med Chem , vol.21 , pp. 295-302
    • Souto, A.1    Montaos, M.A.2    Balado, M.3    Osorio, C.R.4    Rodriguez, J.5    Lemos, M.L.6    Jimenez, C.7
  • 171
    • 0031750326 scopus 로고    scopus 로고
    • The synthesis and antibacterial activity of two pyoverdin-ampicillin conjugates, entering Pseudomonas aeruginosa via the pyoverdin-mediated iron uptake pathway
    • Kinzel O, Tappe R, Gerus I, Budzikiewicz H (1998) The synthesis and antibacterial activity of two pyoverdin-ampicillin conjugates, entering Pseudomonas aeruginosa via the pyoverdin-mediated iron uptake pathway. J Antibiot 51:499–507. doi:10.7164/antibiotics. 51.499
    • (1998) J Antibiot , vol.51 , pp. 499-507
    • Kinzel, O.1    Tappe, R.2    Gerus, I.3    Budzikiewicz, H.4
  • 172
    • 84903954444 scopus 로고    scopus 로고
    • Enterobactin-mediated delivery of β-lactam antibiotics enhances antibacterial activity against pathogenic Escherichia coli
    • Zheng T, Nolan EM (2014) Enterobactin-mediated delivery of β-lactam antibiotics enhances antibacterial activity against pathogenic Escherichia coli. J Am Chem Soc 136:9677–9691. doi:10.1021/ja503911p
    • (2014) J am Chem Soc , vol.136 , pp. 9677-9691
    • Zheng, T.1    Nolan, E.M.2
  • 173
    • 84937145609 scopus 로고    scopus 로고
    • Targeting virulence: salmochelin modification tunes the antibacterial activity spectrum of β-lactams for pathogen-selective killing of Escherichia coli
    • Chairatana P, Zheng T, Nolan EM (2015) Targeting virulence: salmochelin modification tunes the antibacterial activity spectrum of β-lactams for pathogen-selective killing of Escherichia coli. Chem Sci 6:4458–4471. doi:10.1039/C5SC00962F
    • (2015) Chem Sci , vol.6 , pp. 4458-4471
    • Chairatana, P.1    Zheng, T.2    Nolan, E.M.3
  • 174
    • 84934942717 scopus 로고    scopus 로고
    • Clostridium difficile drug pipeline: Challenges in discovery and development of new agents
    • Jarrad AM, Karoli T, Blaskovich MAT, Lyras D, Cooper MA (2015) Clostridium difficile drug pipeline: challenges in discovery and development of new agents. J Med Chem 58:5164–5185. doi:10.1021/jm5016846
    • (2015) J Med Chem , vol.58 , pp. 5164-5185
    • Jarrad, A.M.1    Karoli, T.2    Blaskovich, M.A.T.3    Lyras, D.4    Cooper, M.A.5
  • 175
    • 85021770759 scopus 로고    scopus 로고
    • Structure-function studies of acinetobactin analogs
    • Shapiro J, Wencewicz TA (2017) Structure-function studies of acinetobactin analogs. Metallomics. doi:10.1039/c7mt00064b
    • (2017) Metallomics
    • Shapiro, J.1    Wencewicz, T.A.2
  • 176
    • 0033049572 scopus 로고    scopus 로고
    • Synthesis and biological evaluation of a pyoverdin-β-lactam conjugate: A new type of arginine-specific cross-linking in aqueous solution
    • Kinzel O, Budzikiewicz H (1999) Synthesis and biological evaluation of a pyoverdin-β-lactam conjugate: a new type of arginine-specific cross-linking in aqueous solution. J Pept Res 53:618–625. doi:10.1034/j.1399-3011.1999.00053.x
    • (1999) J Pept Res , vol.53 , pp. 618-625
    • Kinzel, O.1    Budzikiewicz, H.2
  • 177
    • 0035927431 scopus 로고    scopus 로고
    • Synthesis and activities of pyoverdin-quinolone adducts: A prospective approach to a specific therapy against Pseudomonas aeruginosa
    • Hennard C, Truong QC, Desnottes JF, Paris JM, Moreau NJ, Abdallah MA (2001) Synthesis and activities of pyoverdin-quinolone adducts: a prospective approach to a specific therapy against Pseudomonas aeruginosa. J Med Chem 44:2139–2151. doi:10.1021/jm990508g
    • (2001) J Med Chem , vol.44 , pp. 2139-2151
    • Hennard, C.1    Truong, Q.C.2    Desnottes, J.F.3    Paris, J.M.4    Moreau, N.J.5    Abdallah, M.A.6
  • 178
    • 85018507420 scopus 로고    scopus 로고
    • Iron release from the siderophore pyoverdine in Pseudomonas aeruginosa involves three new actors: FpvC, FpvG, and FpvH
    • Epub ahead of print
    • Ganne G, Brillet K, Basta B, Roche B, Hoegy F, Gasser V, Schalk IJ (2017) Iron release from the siderophore pyoverdine in Pseudomonas aeruginosa involves three new actors: FpvC, FpvG, and FpvH. ACS Chem Biol. doi:10.1021/acschembio.6b01077 (Epub ahead of print)
    • (2017) ACS Chem Biol
    • Ganne, G.1    Brillet, K.2    Basta, B.3    Roche, B.4    Hoegy, F.5    Gasser, V.6    Schalk, I.J.7
  • 179
    • 84944150976 scopus 로고    scopus 로고
    • Evaluation of (Acyloxy)alkyl ester linkers for antibiotic release from siderophore–antibiotic conjugates
    • Zheng T, Nolan EM (2015) Evaluation of (acyloxy)alkyl ester linkers for antibiotic release from siderophore–antibiotic conjugates. Bioorg Med Chem Lett 25:4987–4991. doi:10.1016/j.bmcl.2015.02.034
    • (2015) Bioorg Med Chem Lett , vol.25 , pp. 4987-4991
    • Zheng, T.1    Nolan, E.M.2
  • 180
    • 84861580404 scopus 로고    scopus 로고
    • Chemical syntheses and in vitro antibacterial activity of two desferrioxamine B-ciprofloxacin conjugates with potential esterase and phosphatase triggered drug release linkers
    • Ji C, Miller MJ (2012) Chemical syntheses and in vitro antibacterial activity of two desferrioxamine B-ciprofloxacin conjugates with potential esterase and phosphatase triggered drug release linkers. Bioorg Med Chem 20:3828–3836. doi:10.1016/j.bmc.2012.04.034
    • (2012) Bioorg Med Chem , vol.20 , pp. 3828-3836
    • Ji, C.1    Miller, M.J.2
  • 181
    • 84940002596 scopus 로고    scopus 로고
    • Siderophore–fluoroquinolone conjugates containing potential reduction-triggered linkers for drug release: Synthesis and antibacterial activity
    • Ji C, Miller MJ (2015) Siderophore–fluoroquinolone conjugates containing potential reduction-triggered linkers for drug release: synthesis and antibacterial activity. Biometals 28:541–551. doi:10.1007/s10534-015-9830-3
    • (2015) Biometals , vol.28 , pp. 541-551
    • Ji, C.1    Miller, M.J.2
  • 182
    • 9744232909 scopus 로고    scopus 로고
    • Time-related differences in the physical property profiles of oral drugs
    • Leeson PD, Davis AM (2004) Time-related differences in the physical property profiles of oral drugs. J Med Chem 47:6338–6348. https://doi.org/10.1021/jm049717d
    • (2004) J Med Chem , vol.47 , pp. 6338-6348
    • Leeson, P.D.1    Davis, A.M.2
  • 183
    • 78649312737 scopus 로고    scopus 로고
    • Selective capture and identification of pathogenic bacteria using an immobilized siderophore
    • Doorneweerd DD, Henne WA, Reifenberger RG, Low PS (2010) Selective capture and identification of pathogenic bacteria using an immobilized siderophore. Langmuir 26:15424–15429. doi:10.1021/la101962w
    • (2010) Langmuir , vol.26 , pp. 15424-15429
    • Doorneweerd, D.D.1    Henne, W.A.2    Reifenberger, R.G.3    Low, P.S.4
  • 184
    • 84957566014 scopus 로고    scopus 로고
    • Determination of bacterial viability by selective capture using surface-bound siderophores
    • Wolfenden M, Sakamuri R, Anderson A, Prasad L, Schmidt J, Mukundan H (2012) Determination of bacterial viability by selective capture using surface-bound siderophores. Adv Biol Chem 2:396–402. doi:10.4236/abc.2012.24049
    • (2012) Adv Biol Chem , vol.2 , pp. 396-402
    • Wolfenden, M.1    Sakamuri, R.2    Anderson, A.3    Prasad, L.4    Schmidt, J.5    Mukundan, H.6
  • 185
    • 84865484360 scopus 로고    scopus 로고
    • Siderophore-based detection of Fe(Iii) and microbial pathogens
    • Zheng T, Nolan EM (2012) Siderophore-based detection of Fe(iii) and microbial pathogens. Metallomics 4:866–880. doi:10.1039/C2MT20082A
    • (2012) Metallomics , vol.4 , pp. 866-880
    • Zheng, T.1    Nolan, E.M.2
  • 186
    • 84957601838 scopus 로고    scopus 로고
    • Rapid identification of Pseudomonas spp. Via Raman spectroscopy using pyoverdine as capture probe
    • Pahlow S, St€ockel S, Pollok S, Cialla-May D, R€osch P, Weber K, Popp J (2016) Rapid identification of Pseudomonas spp. via Raman spectroscopy using pyoverdine as capture probe. Anal Chem 88:1570–1577. doi:10.1021/acs.analchem.5b02829
    • (2016) Anal Chem , vol.88 , pp. 1570-1577
    • Pahlow, S.1    St€Ockel, S.2    Pollok, S.3    Cialla-May, D.4    R€Osch, P.5    Weber, K.6    Popp, J.7
  • 187
    • 84984911619 scopus 로고    scopus 로고
    • Siderophores as molecular tools in medical and environmental applications
    • Kurth C, Kage H, Nett M (2016) Siderophores as molecular tools in medical and environmental applications. Org Biomol Chem 14:8212–8227. doi:10.1039/C6OB01400C
    • (2016) Org Biomol Chem , vol.14 , pp. 8212-8227
    • Kurth, C.1    Kage, H.2    Nett, M.3
  • 188
    • 84925796249 scopus 로고    scopus 로고
    • Beyond iron: Non-classical biological functions of bacterial siderophores
    • Johnstone TC, Nolan EM (2015) Beyond iron: non-classical biological functions of bacterial siderophores. Dalton Trans 44:6320–6339. doi:10.1039/c4dt03559c
    • (2015) Dalton Trans , vol.44 , pp. 6320-6339
    • Johnstone, T.C.1    Nolan, E.M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.