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Volumn 56, Issue 11, 2012, Pages 5821-5830

Targeting the substrate preference of a type I nitroreductase to develop antitrypanosomal quinone-based prodrugs

Author keywords

[No Author keywords available]

Indexed keywords

2 AMINO 5 (1 METHYL 5 NITRO 2 IMIDAZOLYL) 1,3,4 THIADIAZOLE; 6,7 DIHYDRO 2 NITRO 6 (4 TRIFLUOROMETHOXYBENZYLOXY) 5H IMIDAZO[2,1 B][1,3]OXAZINE; ANTITRYPANOSOMAL AGENT; AZIRIDINYLBENZOQUINONE; BENZNIDAZOLE; DUROQUINONE; METRONIDAZOLE; NIFURTIMOX; NITROBENZYLTHIOGUANOSINE; NITROFURAL; NITROFURANTOIN; NITROREDUCTASE; PRODRUG; QUINONE DERIVATIVE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE (UBIQUINONE); UBIQUINONE;

EID: 84868019328     PISSN: 00664804     EISSN: 10986596     Source Type: Journal    
DOI: 10.1128/AAC.01227-12     Document Type: Article
Times cited : (28)

References (68)
  • 1
    • 84856955769 scopus 로고    scopus 로고
    • High-throughput decoding of antitrypanosomal drug efficacy and resistance
    • Alsford S, et al. 2012. High-throughput decoding of antitrypanosomal drug efficacy and resistance. Nature 482:232-236.
    • (2012) Nature , vol.482 , pp. 232-236
    • Alsford, S.1
  • 2
    • 27644517022 scopus 로고    scopus 로고
    • Tagging a T. brucei rRNA locus improves stable transfection efficiency and circumvents in-ducible expression position effects
    • Alsford S, Kawahara T, Glover L, Horn D. 2005. Tagging a T. brucei rRNA locus improves stable transfection efficiency and circumvents in-ducible expression position effects. Mol. Biochem. Parasitol. 144:142-148.
    • (2005) Mol. Biochem. Parasitol. , vol.144 , pp. 142-148
    • Alsford, S.1    Kawahara, T.2    Glover, L.3    Horn, D.4
  • 3
    • 0000853187 scopus 로고
    • The molar extinction coefficient of 2,6-dichlorophenol indophenol
    • Armstrong JM. 1964. The molar extinction coefficient of 2,6-dichlorophenol indophenol. Biochim. Biophy. Acta 86:194-197.
    • (1964) Biochim. Biophy. Acta , vol.86 , pp. 194-197
    • Armstrong, J.M.1
  • 4
    • 0034321937 scopus 로고    scopus 로고
    • Clinical applications of quinone-containing alkylating agents
    • Begleiter A. 2000. Clinical applications of quinone-containing alkylating agents. Front. Biosci. 5:E153-E171.
    • (2000) Front. Biosci. , vol.5
    • Begleiter, A.1
  • 5
    • 70149108335 scopus 로고    scopus 로고
    • An estimate of the burden of Chagas disease in the United States
    • Bern C, Montgomery SP. 2009. An estimate of the burden of Chagas disease in the United States. Clin. Infect. Dis. 49:e52-e54.
    • (2009) Clin. Infect. Dis. , vol.49
    • Bern, C.1    Montgomery, S.P.2
  • 6
    • 0027259298 scopus 로고
    • Non-cytochrome mediated mitochondrial ATP production in bloodstream form Trypanosoma brucei brucei
    • Bienen EJ, Maturi RK, Pollakis G, Clarkson AB, Jr. 1993. Non-cytochrome mediated mitochondrial ATP production in bloodstream form Trypanosoma brucei brucei. Eur. J. Biochem. 216:75-80.
    • (1993) Eur. J. Biochem. , vol.216 , pp. 75-80
    • Bienen, E.J.1    Maturi, R.K.2    Pollakis, G.3    Clarkson Jr., A.B.4
  • 7
    • 77957374117 scopus 로고    scopus 로고
    • Trypanocidal activity of aziridinyl nitrobenzamide prodrugs
    • Bot C, et al. 2010. Trypanocidal activity of aziridinyl nitrobenzamide prodrugs. Antimicrob. Agents Chemother. 54:4246-4252.
    • (2010) Antimicrob. Agents Chemother. , vol.54 , pp. 4246-4252
    • Bot, C.1
  • 8
  • 9
    • 0025892415 scopus 로고
    • Purification and characterization of an oxygen-insensitive NAD(P)H nitroreductase from Enterobacter cloacae
    • Bryant C, DeLuca M. 1991. Purification and characterization of an oxygen-insensitive NAD(P)H nitroreductase from Enterobacter cloacae. J. Biol. Chem. 266:4119-4125.
    • (1991) J. Biol. Chem. , vol.266 , pp. 4119-4125
    • Bryant, C.1    DeLuca, M.2
  • 10
    • 33748309413 scopus 로고    scopus 로고
    • Trypanosome alternative oxidase: From molecule to function
    • Chaudhuri M, Ott RD, Hill GC. 2006. Trypanosome alternative oxidase: from molecule to function. Trends Parasitol. 22:484-491.
    • (2006) Trends Parasitol. , vol.22 , pp. 484-491
    • Chaudhuri, M.1    Ott, R.D.2    Hill, G.C.3
  • 11
    • 58849153727 scopus 로고    scopus 로고
    • Design of anticancer prodrugs for reductive activation
    • Chen Y, Hu L. 2009. Design of anticancer prodrugs for reductive activation. Med. Res. Rev. 29:29-64.
    • (2009) Med. Res. Rev. , vol.29 , pp. 29-64
    • Chen, Y.1    Hu, L.2
  • 12
    • 0024419431 scopus 로고
    • Respiration of bloodstream forms of the parasiteTrypanosoma brucei brucei is dependent on a plant-like alternative oxidase
    • Clarkson AB, Jr, Bienen EJ, Pollakis G, Grady RW. 1989. Respiration of bloodstream forms of the parasiteTrypanosoma brucei brucei is dependent on a plant-like alternative oxidase. J. Biol. Chem. 264:17770-17776.
    • (1989) J. Biol. Chem. , vol.264 , pp. 17770-17776
    • Clarkson Jr., A.B.1    Bienen, E.J.2    Pollakis, G.3    Grady, R.W.4
  • 13
    • 34548572724 scopus 로고    scopus 로고
    • Validation of the comet-X assay as a pharmacodynamic assay for measuring DNA cross-linking produced by the novel anticancer agent RH1 during a phase I clinical trial
    • Danson S, Ranson M, Denneny O, Cummings J, Ward TH. 2007. Validation of the comet-X assay as a pharmacodynamic assay for measuring DNA cross-linking produced by the novel anticancer agent RH1 during a phase I clinical trial. Cancer Chemother. Pharmacol. 60:851-861.
    • (2007) Cancer Chemother. Pharmacol. , vol.60 , pp. 851-861
    • Danson, S.1    Ranson, M.2    Denneny, O.3    Cummings, J.4    Ward, T.H.5
  • 14
    • 79957503402 scopus 로고    scopus 로고
    • Phase I pharmacokinetic and pharmacodynamic study of the bioreductive drug RH1
    • Danson SJ, et al. 2011. Phase I pharmacokinetic and pharmacodynamic study of the bioreductive drug RH1. Ann. Oncol. 22:1653-1660.
    • (2011) Ann. Oncol. , vol.22 , pp. 1653-1660
    • Danson, S.J.1
  • 15
    • 50549169947 scopus 로고
    • DT diaphorase. I. Purification from the soluble fraction of rat-liver cytoplasm, and properties
    • Ernster L, Danielson L, Ljunggren M. 1962. DT diaphorase. I. Purification from the soluble fraction of rat-liver cytoplasm, and properties. Biochim. Biophys. Acta 58:171-188.
    • (1962) Biochim. Biophys. Acta , vol.58 , pp. 171-188
    • Ernster, L.1    Danielson, L.2    Ljunggren, M.3
  • 16
    • 0015881843 scopus 로고
    • A rapid micromethod for determination of FMN and FAD in mixtures
    • Faeder EJ, Siegel LM. 1973. A rapid micromethod for determination of FMN and FAD in mixtures. Anal. Biochem. 53:332-336.
    • (1973) Anal. Biochem. , vol.53 , pp. 332-336
    • Faeder, E.J.1    Siegel, L.M.2
  • 17
    • 0037374119 scopus 로고    scopus 로고
    • Identification of a gene encoding a 54 kDa alternative NADH dehydrogenase in Trypanosoma brucei
    • Fang J, Beattie DS. 2003. Identification of a gene encoding a 54 kDa alternative NADH dehydrogenase in Trypanosoma brucei. Mol. Biochem. Parasitol. 127:73-77.
    • (2003) Mol. Biochem. Parasitol. , vol.127 , pp. 73-77
    • Fang, J.1    Beattie, D.S.2
  • 18
    • 0037022830 scopus 로고    scopus 로고
    • Novel FMN-containing rotenone-insensitive NADH dehydrogenase from Trypanosoma brucei mitochondria: Isolation and characterization
    • Fang J, Beattie DS. 2002. Novel FMN-containing rotenone-insensitive NADH dehydrogenase from Trypanosoma brucei mitochondria: isolation and characterization. Biochemistry 41:3065-3072.
    • (2002) Biochemistry , vol.41 , pp. 3065-3072
    • Fang, J.1    Beattie, D.S.2
  • 19
    • 0037189931 scopus 로고    scopus 로고
    • Rotenone-insensitive NADH dehydrogenase is a potential source of superoxide in procyclic Trypanosoma brucei mitochondria
    • Fang J, Beattie DS. 2002. Rotenone-insensitive NADH dehydrogenase is a potential source of superoxide in procyclic Trypanosoma brucei mitochondria. Mol. Biochem. Parasitol. 123:135-142.
    • (2002) Mol. Biochem. Parasitol. , vol.123 , pp. 135-142
    • Fang, J.1    Beattie, D.S.2
  • 20
    • 0034825865 scopus 로고    scopus 로고
    • Isolation and characterization of complex I, rotenone-sensitive NADH: Ubiquinone oxidoreductase, from the procyclic forms of Trypanosoma brucei
    • Fang J, Wang Y, Beattie DS. 2001. Isolation and characterization of complex I, rotenone-sensitive NADH: ubiquinone oxidoreductase, from the procyclic forms of Trypanosoma brucei. Eur. J. Biochem. 268:3075-3082.
    • (2001) Eur. J. Biochem. , vol.268 , pp. 3075-3082
    • Fang, J.1    Wang, Y.2    Beattie, D.S.3
  • 21
    • 77954761645 scopus 로고    scopus 로고
    • Identification, cloning and characterization of an aldo-keto reductase from Trypanosoma cruzi with quinone oxidoreductase activity
    • Garavaglia PA, et al. 2010. Identification, cloning and characterization of an aldo-keto reductase from Trypanosoma cruzi with quinone oxidoreductase activity. Mol. Biochem. Parasitol. 173:132-141.
    • (2010) Mol. Biochem. Parasitol. , vol.173 , pp. 132-141
    • Garavaglia, P.A.1
  • 22
    • 77953023715 scopus 로고    scopus 로고
    • Chagas disease in Spain, the United States and other non-endemic countries
    • Gascon J, Bern C, Pinazo MJ. 2009. Chagas disease in Spain, the United States and other non-endemic countries. Acta Trop. 115:22-27.
    • (2009) Acta Trop. , vol.115 , pp. 22-27
    • Gascon, J.1    Bern, C.2    Pinazo, M.J.3
  • 23
    • 79958091494 scopus 로고    scopus 로고
    • Imported human African trypanosomiasis in Europe, 2005-2009
    • for EuroTravNet pii=19327
    • Gautret P, et al for EuroTravNet. 2009. Imported human African trypanosomiasis in Europe, 2005-2009. Euro. Surveill. 14: pii=19327. http://www.eurosurveillance.org/ViewArticle.aspx?ArticleId=19327.
    • (2009) Euro. Surveill. , vol.14
    • Gautret, P.1
  • 24
    • 0031953727 scopus 로고    scopus 로고
    • Metronidazole resistance in Helicobacter pylori is due to null mutations in a gene (rdxA) that encodes an oxygen-insensitive NADPH nitroreductase
    • Goodwin A, et al. 1998. Metronidazole resistance in Helicobacter pylori is due to null mutations in a gene (rdxA) that encodes an oxygen-insensitive NADPH nitroreductase. Mol. Microbiol. 28:383-393.
    • (1998) Mol. Microbiol. , vol.28 , pp. 383-393
    • Goodwin, A.1
  • 25
    • 33747792434 scopus 로고    scopus 로고
    • The mitochondrial FAD-dependent glycerol-3-phosphate dehydrogenase of Trypanosomatidae and the glycosomal redox balance of insect stages of Trypanosoma brucei and Leishmania spp
    • Guerra DG, Decottignies A, Bakker BM, Michels PA. 2006. The mitochondrial FAD-dependent glycerol-3-phosphate dehydrogenase of Trypanosomatidae and the glycosomal redox balance of insect stages of Trypanosoma brucei and Leishmania spp. Mol. Biochem. Parasitol. 149: 155-169.
    • (2006) Mol. Biochem. Parasitol. , vol.149 , pp. 155-169
    • Guerra, D.G.1    Decottignies, A.2    Bakker, B.M.3    Michels, P.A.4
  • 26
    • 79953882988 scopus 로고    scopus 로고
    • Nifurtimox activation by trypano-somal type I nitroreductases generates cytotoxic nitrile metabolites
    • Hall BS, Bot C, Wilkinson SR. 2011. Nifurtimox activation by trypano-somal type I nitroreductases generates cytotoxic nitrile metabolites. J. Biol. Chem. 286:13088-13095.
    • (2011) J. Biol. Chem. , vol.286 , pp. 13088-13095
    • Hall, B.S.1    Bot, C.2    Wilkinson, S.R.3
  • 27
    • 84455170162 scopus 로고    scopus 로고
    • Activation of benznidazole by trypano-somal type I nitroreductases results in glyoxal formation
    • Hall BS, Wilkinson SR. 2012. Activation of benznidazole by trypano-somal type I nitroreductases results in glyoxal formation. Antimicrob. Agents Chemother. 56:115-123.
    • (2012) Antimicrob. Agents Chemother. , vol.56 , pp. 115-123
    • Hall, B.S.1    Wilkinson, S.R.2
  • 28
    • 77149159732 scopus 로고    scopus 로고
    • Exploiting the drug-activating properties of a novel trypanosomal nitroreductase
    • Hall BS, Wu X, Hu L, Wilkinson SR. 2010. Exploiting the drug-activating properties of a novel trypanosomal nitroreductase. Antimicrob. Agents Chemother. 54:1193-1199.
    • (2010) Antimicrob. Agents Chemother. , vol.54 , pp. 1193-1199
    • Hall, B.S.1    Wu, X.2    Hu, L.3    Wilkinson, S.R.4
  • 29
    • 0023810590 scopus 로고
    • "Subversive" substrates for the enzyme trypanothione disulfide reductase: Alternative approach to chemotherapy of Chagas disease
    • Henderson GB, et al. 1988. "Subversive" substrates for the enzyme trypanothione disulfide reductase: alternative approach to chemotherapy of Chagas disease. Proc. Natl. Acad. Sci. U. S. A. 85:5374-5378.
    • (1988) Proc. Natl. Acad. Sci. U. S. A. , vol.85 , pp. 5374-5378
    • Henderson, G.B.1
  • 30
    • 0024948840 scopus 로고
    • Continuous cultivation of Trypanosoma brucei blood stream forms in a medium containing a low concentration of serum protein without feeder cell layers
    • Hirumi H, Hirumi K. 1989. Continuous cultivation of Trypanosoma brucei blood stream forms in a medium containing a low concentration of serum protein without feeder cell layers. J. Parasitol. 75:985-989.
    • (1989) J. Parasitol. , vol.75 , pp. 985-989
    • Hirumi, H.1    Hirumi, K.2
  • 31
    • 3042819882 scopus 로고    scopus 로고
    • Natural products active against African trypanosomes: A step towards new drugs
    • Hoet S, Opperdoes F, Brun R, Quetin-Leclercq J. 2004. Natural products active against African trypanosomes: a step towards new drugs. Nat. Prod. Rep. 21:353-364.
    • (2004) Nat. Prod. Rep. , vol.21 , pp. 353-364
    • Hoet, S.1    Opperdoes, F.2    Brun, R.3    Quetin-Leclercq, J.4
  • 32
    • 79958709444 scopus 로고    scopus 로고
    • Synthesis and structure-activity relationships of nitrobenzyl phosphoramide mustards as nitroreductase-activated prodrugs
    • Hu LQ, et al. 2011. Synthesis and structure-activity relationships of nitrobenzyl phosphoramide mustards as nitroreductase-activated prodrugs. Bioorg. Med. Chem. Lett. 21:3986-3991.
    • (2011) Bioorg. Med. Chem. Lett. , vol.21 , pp. 3986-3991
    • Hu, L.Q.1
  • 33
    • 0014842505 scopus 로고
    • One-electron-transfer reactions in biochemical systems. V. Difference in the mechanism of quinone reduction by the NADH dehydrogenase and the NAD(P)H dehydrogenase (DT-diaphorase)
    • Iyanagi T, Yamazaki I. 1970. One-electron-transfer reactions in biochemical systems. V. Difference in the mechanism of quinone reduction by the NADH dehydrogenase and the NAD(P)H dehydrogenase (DT-diaphorase). Biochim. Biophys. Acta 216:282-294.
    • (1970) Biochim. Biophys. Acta , vol.216 , pp. 282-294
    • Iyanagi, T.1    Yamazaki, I.2
  • 34
    • 0033800922 scopus 로고    scopus 로고
    • Regulation of genes encoding NAD(P)H: Quinone oxi-doreductases
    • Jaiswal AK. 2000. Regulation of genes encoding NAD(P)H: quinone oxi-doreductases. Free Radic. Biol. Med. 29:254-262.
    • (2000) Free Radic. Biol. Med. , vol.29 , pp. 254-262
    • Jaiswal, A.K.1
  • 35
    • 68849127873 scopus 로고    scopus 로고
    • Steady-state and stoppedflow kinetic studies of three Escherichia coli NfsB mutants with enhanced activity for the prodrug CB1954
    • Jarrom D, et al. 2009. Steady-state and stoppedflow kinetic studies of three Escherichia coli NfsB mutants with enhanced activity for the prodrug CB1954. Biochemistry 48:7665-7672.
    • (2009) Biochemistry , vol.48 , pp. 7665-7672
    • Jarrom, D.1
  • 36
    • 0032497385 scopus 로고    scopus 로고
    • Steady-state kinetic mechanism, stereospec-ificity, substrate and inhibitor specificity of Enterobacter cloacae nitroreductase
    • Koder RL, Miller AF. 1998. Steady-state kinetic mechanism, stereospec-ificity, substrate and inhibitor specificity of Enterobacter cloacae nitroreductase. Biochim. Biophys. Acta 1387:395-405.
    • (1998) Biochim. Biophys. Acta , vol.1387 , pp. 395-405
    • Koder, R.L.1    Miller, A.F.2
  • 37
    • 0037020868 scopus 로고    scopus 로고
    • A key role for old yellow enzyme in the metabolism of drugs by Trypanosoma cruzi
    • Kubata BK, et al. 2002. A key role for old yellow enzyme in the metabolism of drugs by Trypanosoma cruzi. J. Exp. Med. 196:1241-1251.
    • (2002) J. Exp. Med. , vol.196 , pp. 1241-1251
    • Kubata, B.K.1
  • 38
    • 34250160202 scopus 로고    scopus 로고
    • A novel Giardia lamblia nitroreductase, GlNR1, interacts with nitazoxanide and other thiazolides
    • Müller J, Wastling J, Sanderson S, Muller N, Hemphill A. 2007. A novel Giardia lamblia nitroreductase, GlNR1, interacts with nitazoxanide and other thiazolides. Antimicrob. Agents Chemother. 51:1979-1986.
    • (2007) Antimicrob. Agents Chemother. , vol.51 , pp. 1979-1986
    • Müller, J.1    Wastling, J.2    Sanderson, S.3    Muller, N.4    Hemphill, A.5
  • 39
    • 79954583944 scopus 로고    scopus 로고
    • Nitroreductase (GlNR1) increases susceptibility of Giardia lamblia and Escherichia coli to nitro drugs
    • Nillius D, Muller J, Muller N. 2011. Nitroreductase (GlNR1) increases susceptibility of Giardia lamblia and Escherichia coli to nitro drugs. J. Antimicrob. Chemother. 66:1029-1035.
    • (2011) J. Antimicrob. Chemother. , vol.66 , pp. 1029-1035
    • Nillius, D.1    Muller, J.2    Muller, N.3
  • 40
    • 0037099606 scopus 로고    scopus 로고
    • Two-electron reduction of quinones by Entero-bacter cloacae NAD(P)H: Nitroreductase: Quantitative structure-activity relationships
    • Nivinskas H, et al. 2002. Two-electron reduction of quinones by Entero-bacter cloacae NAD(P)H: nitroreductase: quantitative structure-activity relationships. Arch. Biochem. Biophys. 403:249-258.
    • (2002) Arch. Biochem. Biophys. , vol.403 , pp. 249-258
    • Nivinskas, H.1
  • 41
    • 0036549786 scopus 로고    scopus 로고
    • Evidence for lateral transfer of genes encoding ferredoxins, nitroreductases, NADH oxidase, and alcohol dehydrogenase 3 from anaerobic prokaryotes to Giardia lamblia and Entamoeba histolytica
    • Nixon JE, et al. 2002. Evidence for lateral transfer of genes encoding ferredoxins, nitroreductases, NADH oxidase, and alcohol dehydrogenase 3 from anaerobic prokaryotes to Giardia lamblia and Entamoeba histolytica. Eukaryot. Cell 1:181-190.
    • (2002) Eukaryot. Cell , vol.1 , pp. 181-190
    • Nixon, J.E.1
  • 42
    • 0026040838 scopus 로고
    • Molecular mechanisms of quinone cytotoxicity
    • O'Brien PJ. 1991. Molecular mechanisms of quinone cytotoxicity. Chem.-Biol. Interact. 80:1-41.
    • (1991) Chem.-biol. Interact. , vol.80 , pp. 1-41
    • O'Brien, P.J.1
  • 43
    • 59749086659 scopus 로고    scopus 로고
    • Giardia, Entamoeba, and Trichomonas enzymes activate metronidazole (nitroreductases) and inactivate metronidazole (nitroimidazole reductases)
    • Pal D, et al. 2009. Giardia, Entamoeba, and Trichomonas enzymes activate metronidazole (nitroreductases) and inactivate metronidazole (nitroimidazole reductases). Antimicrob. Agents Chemother. 53:458-464.
    • (2009) Antimicrob. Agents Chemother. , vol.53 , pp. 458-464
    • Pal, D.1
  • 44
    • 0034609776 scopus 로고    scopus 로고
    • Crystal structure of FMN-dependent nitroreductase from Escherichia coli B: A prodrug-activating enzyme
    • Parkinson GN, Skelly JV, Neidle S. 2000. Crystal structure of FMN-dependent nitroreductase from Escherichia coli B: a prodrug-activating enzyme. J. Med. Chem. 43:3624-3631.
    • (2000) J. Med. Chem. , vol.43 , pp. 3624-3631
    • Parkinson, G.N.1    Skelly, J.V.2    Neidle, S.3
  • 45
    • 0018800960 scopus 로고
    • Oxygen-sensitive and -insensitive nitroreduction byEscherichia coli and rat hepatic microsomes
    • Peterson FJ, Mason RP, Hovsepian J, Holtzman JL. 1979. Oxygen-sensitive and -insensitive nitroreduction byEscherichia coli and rat hepatic microsomes. J. Biol. Chem. 254:4009-4014.
    • (1979) J. Biol. Chem. , vol.254 , pp. 4009-4014
    • Peterson, F.J.1    Mason, R.P.2    Hovsepian, J.3    Holtzman, J.L.4
  • 46
    • 73349111624 scopus 로고    scopus 로고
    • The trypanocidal activity of naphthoqui-nones: A review
    • Pinto AV, de Castro SL. 2009. The trypanocidal activity of naphthoqui-nones: a review. Molecules 14:4570-4590.
    • (2009) Molecules , vol.14 , pp. 4570-4590
    • Pinto, A.V.1    De Castro, S.L.2
  • 47
    • 0024592332 scopus 로고
    • Free radical formation by antitumor quinones
    • Powis G. 1989. Free radical formation by antitumor quinones. Free Rad. Biol. Med. 6:63-101.
    • (1989) Free Rad. Biol. Med. , vol.6 , pp. 63-101
    • Powis, G.1
  • 48
    • 0036175346 scopus 로고    scopus 로고
    • Identification of a Mycobacterium tuberculosis putative classical nitroreductase gene whose expression is coregulated with that of the acr aene within macrophages, in standing versus shaking cultures, and under low oxygen conditions
    • Purkayastha A, McCue LA, McDonough KA. 2002. Identification of a Mycobacterium tuberculosis putative classical nitroreductase gene whose expression is coregulated with that of the acr aene within macrophages, in standing versus shaking cultures, and under low oxygen conditions. Infect. Immun. 70:1518-1529.
    • (2002) Infect. Immun. , vol.70 , pp. 1518-1529
    • Purkayastha, A.1    McCue, L.A.2    McDonough, K.A.3
  • 49
    • 17144417314 scopus 로고    scopus 로고
    • Structural and mechanistic studies of Escherichia coli nitroreductase with the antibiotic nitrofurazone. Reversed binding orientations in different redox states of the enzyme
    • Race PR, et al. 2005. Structural and mechanistic studies of Escherichia coli nitroreductase with the antibiotic nitrofurazone. Reversed binding orientations in different redox states of the enzyme. J. Biol. Chem. 280:13256-13264.
    • (2005) J. Biol. Chem. , vol.280 , pp. 13256-13264
    • Race, P.R.1
  • 50
    • 34047136503 scopus 로고    scopus 로고
    • Kinetic and structural characterisation of Escherichia coli nitroreductase mutants showing improved efficacy for the prodrug substrate CB1954
    • Race PR, et al. 2007. Kinetic and structural characterisation of Escherichia coli nitroreductase mutants showing improved efficacy for the prodrug substrate CB1954. J. Mol. Biol. 368:481-492.
    • (2007) J. Mol. Biol. , vol.368 , pp. 481-492
    • Race, P.R.1
  • 51
    • 67651091668 scopus 로고    scopus 로고
    • 2,3-Diphenyl-1,4-naphthoquinone: A potential chemotherapeutic agent against Trypanosoma cruzi
    • Ramos EI, et al. 2009. 2,3-Diphenyl-1,4-naphthoquinone: a potential chemotherapeutic agent against Trypanosoma cruzi. J. Parasitol. 95:461-466.
    • (2009) J. Parasitol. , vol.95 , pp. 461-466
    • Ramos, E.I.1
  • 52
    • 77950824213 scopus 로고    scopus 로고
    • Chagas disease
    • Rassi A, Marin-Neto JA. 2010. Chagas disease. Lancet 375:1388-1402.
    • (2010) Lancet , vol.375 , pp. 1388-1402
    • Rassi, A.1    Marin-Neto, J.A.2
  • 53
    • 72849128937 scopus 로고    scopus 로고
    • Use of nfsB, encoding nitrore-ductase, as a reporter gene to determine the mutational spectrum of spontaneous mutations in Neisseria gonorrhoeae
    • doi: 10.1186/1471-2180-9-239
    • Stein DC, Carrizosa E, Dunham S. 2009. Use of nfsB, encoding nitrore-ductase, as a reporter gene to determine the mutational spectrum of spontaneous mutations in Neisseria gonorrhoeae. BMC Microbiol. 9:239. doi: 10.1186/1471-2180-9-239.
    • (2009) BMC Microbiol. , vol.9 , pp. 239
    • Stein, D.C.1    Carrizosa, E.2    Dunham, S.3
  • 54
    • 41849094126 scopus 로고    scopus 로고
    • Kinetoplastids: Related protozoan pathogens, different diseases
    • Stuart K, et al. 2008. Kinetoplastids: related protozoan pathogens, different diseases. J. Clin. Invest. 118:1301-1310.
    • (2008) J. Clin. Invest. , vol.118 , pp. 1301-1310
    • Stuart, K.1
  • 55
    • 84856666096 scopus 로고    scopus 로고
    • Enigmatic presence of mitochondrial complex I in Trypanosoma brucei bloodstream forms
    • Surve S, Heestand M, Panicucci B, Schnaufer A, Parsons M. 2012. Enigmatic presence of mitochondrial complex I in Trypanosoma brucei bloodstream forms. Eukaryot. Cell 11:183-193.
    • (2012) Eukaryot. Cell , vol.11 , pp. 183-193
    • Surve, S.1    Heestand, M.2    Panicucci, B.3    Schnaufer, A.4    Parsons, M.5
  • 56
    • 0019462630 scopus 로고
    • Studies on oxygen-insensitive nitrofuran reduc-tase in Escherichia coli B/r
    • Tatsumi K, et al. 1981. Studies on oxygen-insensitive nitrofuran reduc-tase in Escherichia coli B/r. J. Biochem. 89:855-859.
    • (1981) J. Biochem. , vol.89 , pp. 855-859
    • Tatsumi, K.1
  • 57
    • 0028847678 scopus 로고
    • Active site studies of DT-diaphorase employing artificial flavins
    • Tedeschi G, Chen S, Massey V. 1995. Active site studies of DT-diaphorase employing artificial flavins. J. Biol. Chem. 270:2512-2516.
    • (1995) J. Biol. Chem. , vol.270 , pp. 2512-2516
    • Tedeschi, G.1    Chen, S.2    Massey, V.3
  • 58
    • 0027397584 scopus 로고
    • Protein stability regulates the expression of cytochrome c during the developmental cycle of Trypanosoma brucei
    • Torri AF, Bertrand KI, Hajduk SL. 1993. Protein stability regulates the expression of cytochrome c during the developmental cycle of Trypanosoma brucei. Mol. Biochem. Parasitol. 57:305-315.
    • (1993) Mol. Biochem. Parasitol. , vol.57 , pp. 305-315
    • Torri, A.F.1    Bertrand, K.I.2    Hajduk, S.L.3
  • 59
    • 0023796283 scopus 로고
    • Posttranscriptional regulation of cytochrome c expression during the developmental cycle of Trypanosoma brucei
    • Torri AF, Hajduk SL. 1988. Posttranscriptional regulation of cytochrome c expression during the developmental cycle of Trypanosoma brucei. Mol. Cell. Biol. 8:4625-4633.
    • (1988) Mol. Cell. Biol. , vol.8 , pp. 4625-4633
    • Torri, A.F.1    Hajduk, S.L.2
  • 60
    • 82555184832 scopus 로고    scopus 로고
    • Sleeping sickness in travelers - Do they really sleep?
    • doi:10.1371/journal.pntd.0001358
    • Urech K, Neumayr A, Blum J. 2011. Sleeping sickness in travelers - do they really sleep? PLoS Negl. Trop. Dis. 5:e1358. doi:10.1371/journal.pntd. 0001358.
    • (2011) PLoS Negl. Trop. Dis. , vol.5
    • Urech, K.1    Neumayr, A.2    Blum, J.3
  • 61
    • 17644389892 scopus 로고    scopus 로고
    • Preclinical evaluation of the pharmacodynamic properties of 2,5-diaziridinyl-3-hydroxymethyl-6-methyl-1,4-benzoquinone
    • Ward TH, et al. 2005. Preclinical evaluation of the pharmacodynamic properties of 2,5-diaziridinyl-3-hydroxymethyl-6-methyl-1,4-benzoquinone. Clin. Cancer Res. 11:2695-2701.
    • (2005) Clin. Cancer Res. , vol.11 , pp. 2695-2701
    • Ward, T.H.1
  • 62
    • 0032508631 scopus 로고    scopus 로고
    • Purification and characterization of wild-type and mutant "Classical" nitroreduc-tases of Salmonella typhimurium. L33R mutation greatly diminishes binding of FMN to the nitroreductase of S. typhimurium
    • Watanabe M, Nishino T, Takio K, Sofuni T, Nohmi T. 1998. Purification and characterization of wild-type and mutant "classical" nitroreduc-tases of Salmonella typhimurium. L33R mutation greatly diminishes binding of FMN to the nitroreductase of S. typhimurium. J. Biol. Chem. 273: 23922-23928.
    • (1998) J. Biol. Chem. , vol.273 , pp. 23922-23928
    • Watanabe, M.1    Nishino, T.2    Takio, K.3    Sofuni, T.4    Nohmi, T.5
  • 63
    • 0031771290 scopus 로고    scopus 로고
    • Oxygen-insensitive nitroreductases: Analysis of the roles of nfsA and nfsB in development of resistance to 5-nitrofuran derivatives in Escherichia coli
    • Whiteway J, et al. 1998. Oxygen-insensitive nitroreductases: analysis of the roles of nfsA and nfsB in development of resistance to 5-nitrofuran derivatives in Escherichia coli. J. Bacteriol. 180:5529-5539.
    • (1998) J. Bacteriol. , vol.180 , pp. 5529-5539
    • Whiteway, J.1
  • 64
    • 78751534394 scopus 로고    scopus 로고
    • Trypanocidal drugs: Mechanisms, resistance and new targets
    • Wilkinson SR, Kelly JM. 2009. Trypanocidal drugs: mechanisms, resistance and new targets. Expert Rev. Mol. Med. 11:e31. http://dx.doi.org/10.1017/ S1462399409001252.
    • (2009) Expert Rev. Mol. Med. , vol.11
    • Wilkinson, S.R.1    Kelly, J.M.2
  • 66
    • 57349135857 scopus 로고    scopus 로고
    • Dissecting the role of multiple reductases in bioactivation and cytotoxicity of the antitumor agent 2,5-diaziridinyl-3-(hydroxymethyl)-6-methyl- 1,4-benzoquinone (RH1)
    • Yan C, Kepa JK, Siegel D, Stratford IJ, Ross D. 2008. Dissecting the role of multiple reductases in bioactivation and cytotoxicity of the antitumor agent 2,5-diaziridinyl-3-(hydroxymethyl)-6-methyl-1,4-benzoquinone (RH1). Mol. Pharmacol. 74:1657-1665.
    • (2008) Mol. Pharmacol. , vol.74 , pp. 1657-1665
    • Yan, C.1    Kepa, J.K.2    Siegel, D.3    Stratford, I.J.4    Ross, D.5
  • 67
    • 0029745672 scopus 로고    scopus 로고
    • Biochemical characterization of NfsA, the Escherichia coli major nitroreductase exhibiting a high amino acid sequence homology to Frp, a Vibrio harveyi flavin oxidoreductase
    • Zenno S, et al. 1996. Biochemical characterization of NfsA, the Escherichia coli major nitroreductase exhibiting a high amino acid sequence homology to Frp, a Vibrio harveyi flavin oxidoreductase. J. Bacteriol. 178: 4508-4514.
    • (1996) J. Bacteriol. , vol.178 , pp. 4508-4514
    • Zenno, S.1
  • 68
    • 0029808844 scopus 로고    scopus 로고
    • Gene cloning, purification, and characterization of NfsB, a minor oxygen-insensitive nitroreductase from Escherichia coli, similar in biochemical properties to FRase I, the major flavin reductase in Vibrio fischeri
    • Zenno S, Koike H, Tanokura M, Saigo K. 1996. Gene cloning, purification, and characterization of NfsB, a minor oxygen-insensitive nitroreductase from Escherichia coli, similar in biochemical properties to FRase I, the major flavin reductase in Vibrio fischeri. J. Biochem. 120:736-744.
    • (1996) J. Biochem. , vol.120 , pp. 736-744
    • Zenno, S.1    Koike, H.2    Tanokura, M.3    Saigo, K.4


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