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Volumn 5, Issue 15, 2013, Pages 1861-1875

Structural insights into the enzymes of the trypanothione pathway: Targets for antileishmaniasis drugs

Author keywords

[No Author keywords available]

Indexed keywords

AMIPHENAZOLE; ANTIPROTOZOAL AGENT; AUROTHIOGLUCOSE; AUROTHIOMALATE; BETULIN; GLUTATHIONE DERIVATIVE; GLUTATHIONE SYNTHASE; GOLD COMPLEX; GOLD DERIVATIVE; INDAZOLE DERIVATIVE; MEPACRINE; N BENZOYLOXYCARBONYL (2,4DINITROPHENYL)GLUTATHIONE ESTER; PAULLONE DERIVATIVE; PEROXIDASE; PHENYLPYRAZOLE; PHOSPHINIC ACID DERIVATIVE; PLATINUM COMPLEX; PROCHLORPERAZINE; PROTOZOAL PROTEIN; PYRAZOLE DERIVATIVE; SILVER DERIVATIVE; SPERMIDINE SYNTHASE; TOMATINE; TRIPHENYLTETRAZOLIUM; TRYPANOTHIONE; TRYPANOTHIONE REDUCTASE; TRYPANOTHIONE SYNTHETASE AMIDASE; TRYPAREDOXIN; UNCLASSIFIED DRUG; UNINDEXED DRUG; UVAOL;

EID: 84886497242     PISSN: 17568919     EISSN: 17568927     Source Type: Journal    
DOI: 10.4155/fmc.13.146     Document Type: Review
Times cited : (57)

References (82)
  • 1
    • 33645059434 scopus 로고    scopus 로고
    • The evolution and diversity of kinetoplastid flagellates
    • Simpson AG, Stevens JR, Lukes J. The evolution and diversity of kinetoplastid flagellates. Trends Parasitol. 22(4), 168-174 (2006
    • (2006) Trends Parasitol , vol.22 , Issue.4 , pp. 168-174
    • Simpson, A.G.1    Stevens, J.R.2    Lukes, J.3
  • 2
    • 77954735994 scopus 로고    scopus 로고
    • The WHO. Education is key to controlling visceral leishmaniasis
    • The WHO. Education is key to controlling visceral leishmaniasis. Bull. World Health Organ. 88(1), 11-12 (2010
    • (2010) Bull. World Health Organ , vol.88 , Issue.1 , pp. 11-12
  • 4
    • 34447626703 scopus 로고    scopus 로고
    • Evolutionary and geographical history of the Leishmania donovani complex with a revision of current taxonomy
    • Lukes J, Mauricio IL, Schonian G. et al. Evolutionary and geographical history of the Leishmania donovani complex with a revision of current taxonomy. Proc. Natl Acad. Sci. USA 104(22), 9375-9380 (2007
    • (2007) Proc. Natl Acad. Sci. USA , vol.104 , Issue.22 , pp. 9375-9380
    • Lukes, J.1    Mauricio, I.L.2    Schonian, G.3
  • 5
    • 46349089848 scopus 로고    scopus 로고
    • Spread of vector-borne diseases and neglect of leishmaniasis, europe
    • Dujardin JC, Campino L, Canavate C et al. Spread of vector-borne diseases and neglect of Leishmaniasis, Europe. Emerg. Infect. Dis. 14(7), 1013-1018 (2008
    • (2008) Emerg. Infect. Dis , vol.14 , Issue.7 , pp. 1013-1018
    • Dujardin, J.C.1    Campino, L.2    Canavate, C.3
  • 6
    • 84859804574 scopus 로고    scopus 로고
    • Re-emergence of visceral and cutaneous leishmaniasis in the Greek Island of Crete
    • Christodoulou V, Antoniou M, Ntais P et al. Re-emergence of visceral and cutaneous leishmaniasis in the Greek Island of Crete. Vector Borne Zoonotic Dis. 12(3), 214-222 (2012
    • (2012) Vector Borne Zoonotic Dis , vol.12 , Issue.3 , pp. 214-222
    • Christodoulou, V.1    Antoniou, M.2    Ntais, P.3
  • 7
    • 82555169355 scopus 로고    scopus 로고
    • Combining climatic projections and dispersal ability: A method for estimating the responses of sandfly vector species to climate change
    • Fischer D, Moeller P, Thomas SM, Naucke TJ, Beierkuhnlein C. Combining climatic projections and dispersal ability: A method for estimating the responses of sandfly vector species to climate change. PLoS Negl. Trop. Dis. 5(11), e1407 (2011
    • (2011) PLoS Negl. Trop. Dis , vol.5 , Issue.11
    • Fischer, D.1    Moeller, P.2    Thomas, S.M.3    Naucke, T.J.4    Beierkuhnlein, C.5
  • 8
    • 0035348374 scopus 로고    scopus 로고
    • The increase in risk factors for leishmaniasis worldwide
    • Desjeux P. The increase in risk factors for leishmaniasis worldwide. Trans. R. Soc. Trop. Med. Hyg. 95, 239-243 (2001
    • (2001) Trans. R. Soc. Trop. Med. Hyg , vol.95 , pp. 239-243
    • Desjeux, P.1
  • 9
    • 84863884120 scopus 로고    scopus 로고
    • Leishmania tdr1 structure a unique trimeric glutathione transferase capable of deglutathionylation and antimonial prodrug activation
    • Fyfe PK, Westrop GD, Silva AM, Coombs GH, Hunter WN. Leishmania TDR1 structure, a unique trimeric glutathione transferase capable of deglutathionylation and antimonial prodrug activation. Proc. Natl Acad. Sci. USA 109(29), 11693-11698 (2012
    • (2012) Proc. Natl Acad. Sci. USA , vol.109 , Issue.29 , pp. 11693-11698
    • Fyfe, P.K.1    Westrop, G.D.2    Silva, A.M.3    Coombs, G.H.4    Hunter, W.N.5
  • 10
    • 0033509735 scopus 로고    scopus 로고
    • Evidence that the high incidence of treatment failures in indian kala-Azar is due to the emergence of antimony-resistant strains of leishmania donovani
    • Lira R, Sundar S, Makharia A et al. Evidence that the high incidence of treatment failures in Indian kala-Azar is due to the emergence of antimony-resistant strains of Leishmania donovani. J. Infect. Dis. 180(2), 564-567 (1999
    • (1999) J. Infect. Dis , vol.180 , Issue.2 , pp. 564-567
    • Lira, R.1    Sundar, S.2    Makharia, A.3
  • 11
    • 33744464744 scopus 로고    scopus 로고
    • Unresponsiveness to glucantime treatment in Iranian cutaneous leishmaniasis due to drug-resistant Leishmania tropica parasites
    • Hadighi R, Mohebali M, Boucher P et al. Unresponsiveness to glucantime treatment in Iranian cutaneous leishmaniasis due to drug-resistant Leishmania tropica parasites. PLoS Med. 3(5), e162 (2006
    • (2006) PLoS Med , vol.3 , Issue.5
    • Hadighi, R.1    Mohebali, M.2    Boucher, P.3
  • 12
    • 0034855527 scopus 로고    scopus 로고
    • Resistance to treatment in Kala-Azar: Speciation of isolates from northeast India
    • Sundar S, Pai K, Kumar R et al. Resistance to treatment in Kala-Azar: Speciation of isolates from northeast India. Am. J. Trop. Med. Hyg. 65(3), 193-196 (2001
    • (2001) Am. J. Trop. Med. Hyg , vol.65 , Issue.3 , pp. 193-196
    • Sundar, S.1    Pai, K.2    Kumar, R.3
  • 13
    • 16844369135 scopus 로고    scopus 로고
    • Antimony-resistant Leishmania donovaniin eastern Sudan: Incidence and in vitro correlation
    • Abdo MG, Elamin WM, Khalil EA, Mukhtar MM. Antimony-resistant Leishmania donovaniin eastern Sudan: Incidence and in vitro correlation. East Mediterr. Health J. 9(4), 837-843 (2003
    • (2003) East Mediterr. Health J. , vol.9 , Issue.4 , pp. 837-843
    • Abdo, M.G.1    Elamin, W.M.2    Khalil, E.A.3    Mukhtar, M.M.4
  • 14
    • 0036240055 scopus 로고    scopus 로고
    • Chemotherapy of leishmaniasis
    • Croft SL, Yardley V. Chemotherapy of leishmaniasis. Curr. Pharm. Des. 8, 319-342 (2002
    • (2002) Curr. Pharm. Des , vol.8 , pp. 319-342
    • Croft, S.L.1    Yardley, V.2
  • 15
    • 83055181526 scopus 로고    scopus 로고
    • Therapeutic switching in leishmania chemotherapy: A distinct approach towards unsatisfied treatment needs
    • Shakya N, Bajpai P, Gupta S. Therapeutic switching in leishmania chemotherapy: A distinct approach towards unsatisfied treatment needs. J. Parasit. Dis. 35(2), 104-112 (2011
    • (2011) J. Parasit. Dis , vol.35 , Issue.2 , pp. 104-112
    • Shakya, N.1    Bajpai, P.2    Gupta, S.3
  • 16
    • 0025872527 scopus 로고
    • Liposomal amphotericin B in drug-resistant visceral leishmaniasis
    • Davidson RN, Croft SL, Scott A et al. Liposomal amphotericin B in drug-resistant visceral leishmaniasis. Lancet 337(8749), 1061-1062 (1991
    • (1991) Lancet , vol.337 , Issue.8749 , pp. 1061-1062
    • Davidson, R.N.1    Croft, S.L.2    Scott, A.3
  • 18
    • 22244472295 scopus 로고    scopus 로고
    • Comparative genomics oftrypanosomatid parasitic protozoa
    • El-Sayed NM, Myler PJ, Blandin G et al. Comparative genomics oftrypanosomatid parasitic protozoa. Science 309(5733), 404-409 (2005
    • (2005) Science , vol.309 , Issue.5733 , pp. 404-409
    • El-Sayed, N.M.1    Myler, P.J.2    Blandin, G.3
  • 19
    • 78751591332 scopus 로고    scopus 로고
    • Polyamine metabolism in Leishmania: From arginine to trypanothione
    • Colotti G, Ilari A. Polyamine metabolism in Leishmania: From arginine to trypanothione. Amino Acids 40(2), 269-285 (2011
    • (2011) Amino Acids , vol.40 , Issue.2 , pp. 269-285
    • Colotti, G.1    Ilari, A.2
  • 20
    • 49349112856 scopus 로고    scopus 로고
    • Redox control in trypanosomatids parasitic protozoa with trypanothione-based thiol metabolism
    • Krauth-Siegel RL, Comini MA. Redox control in trypanosomatids parasitic protozoa with trypanothione-based thiol metabolism. Biochim. Biophys. Acta 1780(11), 1236-1248 (2008
    • (2008) Biochim. Biophys. Acta , vol.1780 , Issue.11 , pp. 1236-1248
    • Krauth-Siegel, R.L.1    Comini, M.A.2
  • 21
    • 0022002912 scopus 로고
    • Trypanothione: A novel bis(glutathionyl)spermidine cofactor for glutathione reductase in trypanosomatids
    • Fairlamb AH, Blackburn P, Ulrich P, Chait BT, Cerami A. Trypanothione: A novel bis(glutathionyl)spermidine cofactor for glutathione reductase in trypanosomatids. Science 227(4693), 1485-1487 (1985
    • (1985) Science , vol.227 , Issue.4693 , pp. 1485-1487
    • Fairlamb, A.H.1    Blackburn, P.2    Ulrich, P.3    Chait, B.T.4    Cerami, A.5
  • 23
    • 0030926411 scopus 로고    scopus 로고
    • Disruption of the trypanothione reductase gene of Leishmania decreases its ability to survive oxidative stress in macrophages
    • Dumas C, Ouellette M, Tovar J et al. Disruption of the trypanothione reductase gene of Leishmania decreases its ability to survive oxidative stress in macrophages. EMBO J. 16(10), 2590-2598 (1997
    • (1997) EMBO J , vol.16 , Issue.10 , pp. 2590-2598
    • Dumas, C.1    Ouellette, M.2    Tovar, J.3
  • 24
    • 61349124238 scopus 로고    scopus 로고
    • The cytosolic tryparedoxin of Leishmania infantum is essential for parasite survival
    • Romao S, Castro H, Sousa C, Carvalho S, Tomas AM. The cytosolic tryparedoxin of Leishmania infantum is essential for parasite survival. Int. J. Parasitol. 39, 703-711 (2009
    • (2009) Int. J. Parasitol , vol.39 , pp. 703-711
    • Romao, S.1    Castro, H.2    Sousa, C.3    Carvalho, S.4    Tomas, A.M.5
  • 25
    • 0037518119 scopus 로고    scopus 로고
    • Role of peroxidoxins in Leishmania chagasi survival. Evidence of an enzymatic defense against nitrosative stress
    • Barr SD, Gedamu L. Role of peroxidoxins in Leishmania chagasi survival. Evidence of an enzymatic defense against nitrosative stress. J. Biol. Chem. 278, 10816-10823 (2003
    • (2003) J. Biol. Chem , vol.278 , pp. 10816-10823
    • Barr, S.D.1    Gedamu, L.2
  • 26
    • 33846963220 scopus 로고    scopus 로고
    • Depletion of the thioredoxin homologue tryparedoxin impairs antioxidative defence in African trypanosomes
    • Comini MA, Krauth-Siegel RL, Flohe L. Depletion of the thioredoxin homologue tryparedoxin impairs antioxidative defence in African trypanosomes. Biochem. J. 402, 43-49 (2007
    • (2007) Biochem. J. , vol.402 , pp. 43-49
    • Comini, M.A.1    Krauth-Siegel, R.L.2    Flohe, L.3
  • 27
    • 0038635977 scopus 로고    scopus 로고
    • The role of glutathione peroxidases in trypanosomatids
    • Wilkinson SR, Kelly JM. The role of glutathione peroxidases in trypanosomatids. Biol. Chem. 384, 517-525 (2003
    • (2003) Biol. Chem , vol.384 , pp. 517-525
    • Wilkinson, S.R.1    Kelly, J.M.2
  • 28
    • 80755142192 scopus 로고    scopus 로고
    • The trypanothione system and the opportunities it offers to create drugs for the neglected kinetoplast diseases
    • Flohè L. The trypanothione system and the opportunities it offers to create drugs for the neglected kinetoplast diseases. Biotechnol. Adv. 30, 294-301 (2011
    • (2011) Biotechnol. Adv , vol.30 , pp. 294-301
    • Flohè, L.1
  • 29
    • 73449144111 scopus 로고    scopus 로고
    • Synthesis, inhibition potency, binding mode, and antiprotozoal activities of f luorescent inhibitors of trypanothione reductase based on mepacrine-conjugated diaryl sulfide scaffolds
    • Eberle C, Burkhard JA, Stump B et al. Synthesis, inhibition potency, binding mode, and antiprotozoal activities of f luorescent inhibitors of trypanothione reductase based on mepacrine-conjugated diaryl sulfide scaffolds. ChemMedChem 4, 2034-2044 (2009
    • (2009) ChemMedChem , vol.4 , pp. 2034-2044
    • Eberle, C.1    Burkhard, J.A.2    Stump, B.3
  • 30
    • 79251537792 scopus 로고    scopus 로고
    • Improved inhibitors of trypanothione reductase by combination of motifs: Synthesis, inhibitory potency, binding mode, and antiprotozoal activities
    • Eberle C, Lauber BS, Fankhauser D et al. Improved inhibitors of trypanothione reductase by combination of motifs: Synthesis, inhibitory potency, binding mode, and antiprotozoal activities. ChemMedChem 6, 292-301 (2011
    • (2011) ChemMedChem , vol.6 , pp. 292-301
    • Eberle, C.1    Lauber, B.S.2    Fankhauser, D.3
  • 31
    • 22744459375 scopus 로고    scopus 로고
    • Inhibitors of Trypanosoma cruzi trypanothione reductase revealed by virtual screening and parallel synthesis
    • Meiering S, Inhoff O, Mies J et al. Inhibitors of Trypanosoma cruzi trypanothione reductase revealed by virtual screening and parallel synthesis. J. Med. Chem. 48, 4793-4802 (2005
    • (2005) J. Med. Chem , vol.48 , pp. 4793-4802
    • Meiering, S.1    Inhoff, O.2    Mies, J.3
  • 32
    • 73449124808 scopus 로고    scopus 로고
    • Investigation of trypanothione reductase as a drug target in Trypanosoma brucei
    • Spinks D, Shanks EJ, Cleghorn LA et al. Investigation of trypanothione reductase as a drug target in Trypanosoma brucei. ChemMedChem 4, 2060-2069 (2009
    • (2009) ChemMedChem , vol.4 , pp. 2060-2069
    • Spinks, D.1    Shanks, E.J.2    Cleghorn, L.A.3
  • 33
    • 0033977079 scopus 로고    scopus 로고
    • Trypanosomes lacking trypanothione reductase are avirulent and show increased sensitivity to oxidative stress
    • Krieger S, Schwarz W, Ariyanayagam MR, Fairlamb AH, Krauth-Siegel RL, Clayton C. Trypanosomes lacking trypanothione reductase are avirulent and show increased sensitivity to oxidative stress. Mol. Microbiol. 35(3), 542-552 (2000
    • (2000) Mol. Microbiol , vol.35 , Issue.3 , pp. 542-552
    • Krieger, S.1    Schwarz, W.2    Ariyanayagam, M.R.3    Fairlamb, A.H.4    Krauth-Siegel, R.L.5    Clayton, C.6
  • 34
    • 70350381791 scopus 로고    scopus 로고
    • Dissecting the essentiality of the bifunctional trypanothione synthetase-Amidase in Trypanosoma brucei using chemical and genetic methods
    • Wyllie S, Oza SL, Patterson S et al. Dissecting the essentiality of the bifunctional trypanothione synthetase-Amidase in Trypanosoma brucei using chemical and genetic methods. Mol. Microbiol. 74(3), 529-540 (2009
    • (2009) Mol. Microbiol , vol.74 , Issue.3 , pp. 529-540
    • Wyllie, S.1    Oza, S.L.2    Patterson, S.3
  • 35
    • 84879786172 scopus 로고    scopus 로고
    • Inhibition of leishmania infantum trypanothione reductase by azole-based compounds: A comparative analysis with its physiological substrate by x-ray crystallography
    • Baiocco P, Poce G, Alfonso S et al. Inhibition of leishmania infantum trypanothione reductase by azole-based compounds: A comparative analysis with its physiological substrate by x-ray crystallography. ChemMedChem 8, 1175-1183 (2013
    • (2013) ChemMedChem , vol.8 , pp. 1175-1183
    • Baiocco, P.1    Poce, G.2    Alfonso, S.3
  • 36
    • 47749111316 scopus 로고    scopus 로고
    • Leishmania trypanothione synthetase-Amidase structure reveals a basis for regulation of conflicting synthetic and hydrolytic activities
    • Fyfe PK, Oza SL, Fairlamb AH, Hunter WN. Leishmania trypanothione synthetase-Amidase structure reveals a basis for regulation of conflicting synthetic and hydrolytic activities. J. Biol. Chem. 283(25), 17672-17680 (2008
    • (2008) J. Biol. Chem , vol.283 , Issue.25 , pp. 17672-17680
    • Fyfe, P.K.1    Oza, S.L.2    Fairlamb, A.H.3    Hunter, W.N.4
  • 37
    • 33845691877 scopus 로고    scopus 로고
    • Dual binding sites for translocation catalysis by Escherichia coli glutathionylspermidine synthetase
    • Pai CH, Chiang BY, Ko TP et al. Dual binding sites for translocation catalysis by Escherichia coli glutathionylspermidine synthetase. EMBO J. 25(24), 5970-5982 (2006
    • (2006) EMBO J , vol.25 , Issue.24 , pp. 5970-5982
    • Pai, C.H.1    Chiang, B.Y.2    Ko, T.P.3
  • 38
    • 0029950031 scopus 로고    scopus 로고
    • Structural classification of proteins: New superfamilies
    • Murzin AG. Structural classification of proteins: New superfamilies. Curr. Opin. Struct. Biol. 6(3), 386-394 (1996
    • (1996) Curr. Opin. Struct. Biol , vol.6 , Issue.3 , pp. 386-394
    • Murzin, A.G.1
  • 39
    • 0033564203 scopus 로고    scopus 로고
    • Molecular basis of glutathione synthetase deficiency and a rare gene permutation event
    • Polekhina G, Board PG, Gali RR, Rossjohn J, Parker MW. Molecular basis of glutathione synthetase deficiency and a rare gene permutation event. EMBO J. 18(12), 3204-3213 (1999
    • (1999) EMBO J , vol.18 , Issue.12 , pp. 3204-3213
    • Polekhina, G.1    Board, P.G.2    Gali, R.R.3    Rossjohn, J.4    Parker, M.W.5
  • 40
    • 84874521821 scopus 로고    scopus 로고
    • Molecular dynamics reveal binding mode of glutathionylspermidine by trypanothione synthetase
    • Koch O, Cappel D, Nocker M et al.Molecular dynamics reveal binding mode of glutathionylspermidine by trypanothione synthetase. PLoS ONE 8(2), e56788 (2013
    • (2013) PLoS ONE , vol.8 , Issue.2
    • Koch, O.1    Cappel, D.2    Nocker, M.3
  • 41
    • 0035974742 scopus 로고    scopus 로고
    • QSAR study on the contribution of log P and E(s) to the in vitro antiprotozoal activity of glutathione derivatives
    • Daunes S, D'Silva C, Kendrick H, Yardley V, Croft SL. QSAR study on the contribution of log P and E(s) to the in vitro antiprotozoal activity of glutathione derivatives. J. Med. Chem. 44, 2976-2983 (2001
    • (2001) J. Med. Chem , vol.44 , pp. 2976-2983
    • Daunes, S.1    D'Silva, C.2    Kendrick, H.3    Yardley, V.4    Croft, S.L.5
  • 43
    • 53849103947 scopus 로고    scopus 로고
    • ATP-dependent ligases in trypanothione biosynthesis-kinetics of catalysis and inhibition by phosphinic acid pseudopeptides
    • Oza SL, Chen S, Wyllie S, Coward JK, Fairlamb AH. ATP-dependent ligases in trypanothione biosynthesis-kinetics of catalysis and inhibition by phosphinic acid pseudopeptides. FEBS J. 275(21), 5408-5421 (2008
    • (2008) FEBS J , vol.275 , Issue.21 , pp. 5408-5421
    • Oza, S.L.1    Chen, S.2    Wyllie, S.3    Coward, J.K.4    Fairlamb, A.H.5
  • 44
    • 73649125297 scopus 로고    scopus 로고
    • Chemical validation of trypanothione synthetase, a potential drug target for human trypanosomiasis
    • Torrie LS, Wyllie S, Spinks D et al. Chemical validation of trypanothione synthetase, a potential drug target for human trypanosomiasis. J. Biol. Chem. 284, 36137-36145 (2009
    • (2009) J. Biol. Chem , vol.284 , pp. 36137-36145
    • Torrie, L.S.1    Wyllie, S.2    Spinks, D.3
  • 45
    • 84555188469 scopus 로고    scopus 로고
    • Design, synthesis and biological evaluation of trypanosoma brucei trypanothione synthetase inhibitors
    • Spinks D, Torrie LS, Thompson S et al. Design, synthesis and biological evaluation of Trypanosoma brucei trypanothione synthetase inhibitors. ChemMedChem 7(1), 95-106 (2012
    • (2012) ChemMedChem , vol.7 , Issue.1 , pp. 95-106
    • Spinks, D.1    Torrie, L.S.2    Thompson, S.3
  • 46
    • 80755169608 scopus 로고    scopus 로고
    • Cloning, expression, characterization and inhibition studies on trypanothione synthetase, a drug target enzyme, from Leishmania donovani
    • Saudagar P, Dubey VK. Cloning, expression, characterization and inhibition studies on trypanothione synthetase, a drug target enzyme, from Leishmania donovani. Biol. Chem. 392, 1113-1122 (2011
    • (2011) Biol. Chem , vol.392 , pp. 1113-1122
    • Saudagar, P.1    Dubey, V.K.2
  • 47
    • 63449136128 scopus 로고    scopus 로고
    • Trypanothione reductase from Leishmania infantum: Cloning, expression, purification, crystallization and preliminary x-ray data analysis
    • Baiocco P, Franceschini S, Ilari A, Colotti G. Trypanothione reductase from Leishmania infantum: Cloning, expression, purification, crystallization and preliminary x-ray data analysis. Protein Pept. Lett. 16(2), 196-200 (2009
    • (2009) Protein Pept. Lett , vol.16 , Issue.2 , pp. 196-200
    • Baiocco, P.1    Franceschini, S.2    Ilari, A.3    Colotti, G.4
  • 48
    • 65249133895 scopus 로고    scopus 로고
    • Molecular basis of antimony treatment in leishmaniasis
    • Baiocco P, Colotti G, Franceschini S, Ilari A. Molecular basis of antimony treatment in leishmaniasis. J. Med. Chem. 52(8), 2603-2612 (2009
    • (2009) J. Med. Chem , vol.52 , Issue.8 , pp. 2603-2612
    • Baiocco, P.1    Colotti, G.2    Franceschini, S.3    Ilari, A.4
  • 49
    • 59549088662 scopus 로고    scopus 로고
    • ProtorP: A protein-protein interaction analysis server
    • Reynolds C, Damerell D, Jones S. ProtorP: A protein-protein interaction analysis server. Bioinformatics 25(3), 413-414 (2009
    • (2009) Bioinformatics , vol.25 , Issue.3 , pp. 413-414
    • Reynolds, C.1    Damerell, D.2    Jones, S.3
  • 50
    • 0024421234 scopus 로고
    • Substrate binding and catalysis by glutathione reductase as derived from refined enzyme: Substrate crystal structures at 2 Å resolution
    • Karplus PA, Schulz GE. Substrate binding and catalysis by glutathione reductase as derived from refined enzyme: Substrate crystal structures at 2 Å resolution. J. Mol. Biol. 210(1), 163-180 (1989
    • (1989) J. Mol. Biol , vol.210 , Issue.1 , pp. 163-180
    • Karplus, P.A.1    Schulz, G.E.2
  • 52
    • 50049107805 scopus 로고    scopus 로고
    • Catalytic cycle of human glutathione reductase near 1 Å resolution
    • Berkholz DS, Faber HR, Savvides SN, Karplus PA. Catalytic cycle of human glutathione reductase near 1 Å resolution. J. Mol. Biol. 382(2), 371-384 (2008
    • (2008) J. Mol. Biol , vol.382 , Issue.2 , pp. 371-384
    • Berkholz, D.S.1    Faber, H.R.2    Savvides, S.N.3    Karplus, P.A.4
  • 53
    • 24644456490 scopus 로고    scopus 로고
    • The battle against trypanosomiasis and leishmaniasis: Metal based and natural product inhibitors of trypanothione reductase
    • O'Sullivan MC. The battle against trypanosomiasis and leishmaniasis: Metal based and natural product inhibitors of trypanothione reductase. Curr. Med. Chem. Anti-Infect. Agents 4(4), 355-378 (2005
    • (2005) Curr. Med. Chem. Anti-Infect. Agents , vol.4 , Issue.4 , pp. 355-378
    • O'Sullivan, M.C.1
  • 54
    • 0033602511 scopus 로고    scopus 로고
    • Cytotoxicity of (2,2́:6́,2́́-Terpyridine) platinum(II) complexes to Leishmania donovani, Trypanosoma cruzi, and Trypanosoma brucei
    • Lowe G, Droz AS, Vilaivan T et al. Cytotoxicity of (2,2́:6́, 2́́-Terpyridine) platinum(II) complexes to Leishmania donovani, Trypanosoma cruzi, and Trypanosoma brucei. J. Med. Chem. 42(6), 999-1006 (1999
    • (1999) J. Med. Chem , vol.42 , Issue.6 , pp. 999-1006
    • Lowe, G.1    Droz, A.S.2    Vilaivan, T.3
  • 55
    • 0034649656 scopus 로고    scopus 로고
    • 2,2́:6́,2́́-Terpyridine) platinum(II) complexes are irreversible inhibitors of Trypanosoma cruzi trypanothione reductase but not of human glutathione reductase
    • Bonse S, Richards JM, Ross SA, Lowe G, Krauth-Siegel RL. (2,2́:6́,2́́-Terpyridine) platinum(II) complexes are irreversible inhibitors of Trypanosoma cruzi trypanothione reductase but not of human glutathione reductase. J. Med. Chem. 43(25), 4812-4821 (2000
    • (2000) J. Med. Chem , vol.43 , Issue.25 , pp. 4812-4821
    • Bonse, S.1    Richards, J.M.2    Ross, S.A.3    Lowe, G.4    Krauth-Siegel, R.L.5
  • 56
    • 33845361203 scopus 로고    scopus 로고
    • Synthesis and characterization of [Au(dppz )2]Cl3 DNA interaction studies and biological activity against Leishmania L) mexicana
    • Navarro M, Hernandez C, Colmenares I et al. Synthesis and characterization of [Au(dppz)2]Cl3. DNA interaction studies and biological activity against Leishmania (L) mexicana. J. Inorg. Biochem. 101(1), 111-116 (2007
    • (2007) J. Inorg. Biochem , vol.101 , Issue.1 , pp. 111-116
    • Navarro, M.1    Hernandez, C.2    Colmenares, I.3
  • 57
    • 70349428517 scopus 로고    scopus 로고
    • Synthesis and characterization of a pyridine-2-Thiol n-oxide gold (i) complex with potent antiproliferative effect against trypanosoma cruzi and leishmania sp insight into its mechanism of action
    • Vieites M, Smircich P, Guggeri L et al. Synthesis and characterization of a pyridine-2-Thiol N-oxide gold(I) complex with potent antiproliferative effect against Trypanosoma cruzi and Leishmania sp. insight into its mechanism of action. J. Inorg. Biochem. 103(10), 1300-1306 (2009
    • (2009) J. Inorg. Biochem , vol.103 , Issue.10 , pp. 1300-1306
    • Vieites, M.1    Smircich, P.2    Guggeri, L.3
  • 58
    • 84861660490 scopus 로고    scopus 로고
    • A gold-containing drug against parasitic polyamine metabolism: The x-ray structure of trypanothione reductase from Leishmania infantum in complex with auranofin reveals a dual mechanism of enzyme inhibition
    • Ilari A, Baiocco P, Messori L et al. A gold-containing drug against parasitic polyamine metabolism: The x-ray structure of trypanothione reductase from Leishmania infantum in complex with auranofin reveals a dual mechanism of enzyme inhibition. Amino Acids 42(2-3), 803-811 (2012
    • (2012) Amino Acids , vol.42 , Issue.2-3 , pp. 803-811
    • Ilari, A.1    Baiocco, P.2    Messori, L.3
  • 59
    • 46449096246 scopus 로고    scopus 로고
    • Clinical pharmacology of gold
    • Kean WF, Kean IR. Clinical pharmacology of gold. Inflammopharmacology 16(3), 112-125 (2008
    • (2008) Inflammopharmacology , vol.16 , Issue.3 , pp. 112-125
    • Kean, W.F.1    Kean, I.R.2
  • 60
    • 0030803602 scopus 로고    scopus 로고
    • Interaction of silver nitrate with readily identifiable groups: Relationship to the antibacterial action of silver ions
    • Liau SY, Read DC, Pugh WJ, Furr JR, Russell AD. Interaction of silver nitrate with readily identifiable groups: Relationship to the antibacterial action of silver ions. Lett. Appl. Microbiol. 25(4), 279-283 (1997
    • (1997) Lett. Appl. Microbiol , vol.25 , Issue.4 , pp. 279-283
    • Liau, S.Y.1    Read, D.C.2    Pugh, W.J.3    Furr, J.R.4    Russell, A.D.5
  • 61
    • 79952639221 scopus 로고    scopus 로고
    • Inhibitory effect of silver nanoparticles on trypanothione reductase activity and Leishmania infantum proliferation
    • Baiocco P. Ilari A, Ceci P et al. Inhibitory effect of silver nanoparticles on trypanothione reductase activity and Leishmania infantum proliferation. ACS Med. Chem. Lett. 2, 230-233 (2011
    • (2011) ACS Med. Chem. Lett , vol.2 , pp. 230-233
    • Baiocco, P.1    Ilari, A.2    Ceci, P.3
  • 62
    • 42049109499 scopus 로고    scopus 로고
    • In vitro evaluation of the effectiveness and cytotoxicity of meglumine antimoniate microspheres produced by spray drying against Leishmania infantum
    • Pujals G, Sune-Negre JM, Perez P et al. In vitro evaluation of the effectiveness and cytotoxicity of meglumine antimoniate microspheres produced by spray drying against Leishmania infantum. Parasitol. Res. 102(6), 1243-1247 (2008
    • (2008) Parasitol. Res , vol.102 , Issue.6 , pp. 1243-1247
    • Pujals, G.1    Sune-Negre, J.M.2    Perez, P.3
  • 63
    • 0030057025 scopus 로고    scopus 로고
    • Crystal structure of the Trypanosoma cruzi trypanothione reductase mepacrine complex
    • Jacoby EM, Schlichting I, Lantwin CB, Kabsch W, Krauth-Siegel RL. Crystal structure of the Trypanosoma cruzi trypanothione reductase mepacrine complex. Proteins 24(1), 73-80 (1996
    • (1996) Proteins , vol.24 , Issue.1 , pp. 73-80
    • Jacoby, E.M.1    Schlichting, I.2    Lantwin, C.B.3    Kabsch, W.4    Krauth-Siegel, R.L.5
  • 64
    • 3142719178 scopus 로고    scopus 로고
    • Two interacting binding sites for quinacrine derivatives in the active site of trypanothione reductase: A template for drug design
    • Saravanamuthu A, Vickers TJ, Bond CS, Peterson MR, Hunter WN, Fairlamb AH. Two interacting binding sites for quinacrine derivatives in the active site of trypanothione reductase: A template for drug design. J. Biol. Chem. 279(28), 29493-29500 (2004
    • (2004) J. Biol. Chem , vol.279 , Issue.28 , pp. 29493-29500
    • Saravanamuthu, A.1    Vickers, T.J.2    Bond, C.S.3    Peterson, M.R.4    Hunter, W.N.5    Fairlamb, A.H.6
  • 65
    • 0030773120 scopus 로고    scopus 로고
    • Rational design of selective ligands for trypanothione reductase from Trypanosoma cruzi. Structural effects on the inhibition by dibenzazepines based on imipramine
    • Garforth J, Yin H, McKie JH, Douglas KT, Fairlamb AH. Rational design of selective ligands for trypanothione reductase from Trypanosoma cruzi. Structural effects on the inhibition by dibenzazepines based on imipramine. J. Enzyme Inhib. 12(3), 161-173 (1997
    • (1997) J. Enzyme Inhib , vol.12 , Issue.3 , pp. 161-173
    • Garforth, J.1    Yin, H.2    McKie, J.H.3    Douglas, K.T.4    Fairlamb, A.H.5
  • 66
    • 0033619994 scopus 로고    scopus 로고
    • Inhibition of Trypanosoma cruzi trypanothione reductase by acridines: Kinetic studies and structure-Activity relationships
    • Bonse S, Santelli-Rouvier C, Barbe J, Krauth-Siege, RL. Inhibition of Trypanosoma cruzi trypanothione reductase by acridines: Kinetic studies and structure-Activity relationships. J. Med. Chem. 42(26), 5448-5454 (1999
    • (1999) J. Med. Chem , vol.42 , Issue.26 , pp. 5448-5454
    • Bonse, S.1    Santelli-Rouvier, C.2    Barbe, J.3    Krauth-Siege, R.L.4
  • 67
    • 0035865881 scopus 로고    scopus 로고
    • 2-And 3-substituted 1,4-naphthoquinone derivatives as subversive substrates of trypanothione reductase and lipoamide dehydrogenase from Trypanosoma cruzi: Synthesis and correlation between redox cycling activities and in vitro cytotoxicity
    • Salmon-Chemin L, Buisine E, Yardley V et al. 2-And 3-substituted 1,4-naphthoquinone derivatives as subversive substrates of trypanothione reductase and lipoamide dehydrogenase from Trypanosoma cruzi: Synthesis and correlation between redox cycling activities and in vitro cytotoxicity. J. Med. Chem. 44(4), 548-565 (2001
    • (2001) J. Med. Chem , vol.44 , Issue.4 , pp. 548-565
    • Salmon-Chemin, L.1    Buisine, E.2    Yardley, V.3
  • 68
    • 0035083882 scopus 로고    scopus 로고
    • Specific peptide inhibitors of trypanothione reductase with backbone structures unrelated to that of substrate: Potential rational drug design lead frameworks
    • McKie JH, Garforth J, Jaouhari R et al. Specific peptide inhibitors of trypanothione reductase with backbone structures unrelated to that of substrate: Potential rational drug design lead frameworks. Amino Acids 20(2), 145-153 (2001
    • (2001) Amino Acids , vol.20 , Issue.2 , pp. 145-153
    • McKie, J.H.1    Garforth, J.2    Jaouhari, R.3
  • 69
    • 58149196803 scopus 로고    scopus 로고
    • Diaryl sulfide-based inhibitors of trypanothione reductase: Inhibition potency, revised binding mode and antiprotozoal activities
    • Stump B, Eberle C, Kaiser M et al. Diaryl sulfide-based inhibitors of trypanothione reductase: Inhibition potency, revised binding mode and antiprotozoal activities. Org. Biomol. Chem. 6(21), 3935-3947 (2008
    • (2008) Org. Biomol. Chem , vol.6 , Issue.21 , pp. 3935-3947
    • Stump, B.1    Eberle, C.2    Kaiser, M.3
  • 70
    • 80053920610 scopus 로고    scopus 로고
    • Dihydroquinazolines as a novel class of Trypanosoma brucei trypanothione reductase inhibitors: Discovery, synthesis, and characterization of their binding mode by protein crystallography
    • Patterson S, Alphey MS, Jones DC et al. Dihydroquinazolines as a novel class of Trypanosoma brucei trypanothione reductase inhibitors: Discovery, synthesis, and characterization of their binding mode by protein crystallography. J. Med. Chem. 54(19), 6514-6530 (2011
    • (2011) J. Med. Chem , vol.54 , Issue.19 , pp. 6514-6530
    • Patterson, S.1    Alphey, M.S.2    Jones, D.C.3
  • 71
    • 0242668686 scopus 로고    scopus 로고
    • Peroxiredoxin evolution and the regulation of hydrogen peroxide signaling
    • Wood ZA, Poole LB, Karplus PA. Peroxiredoxin evolution and the regulation of hydrogen peroxide signaling. Science 300(5619), 650-653 (2003
    • (2003) Science , vol.300 , Issue.5619 , pp. 650-653
    • Wood, Z.A.1    Poole, L.B.2    Karplus, P.A.3
  • 72
    • 79952277996 scopus 로고    scopus 로고
    • Targeting trypanothione metabolism in trypanosomatid human parasites
    • Olin-Sandoval V, Moreno-Sanchez R, Saavedra E. Targeting trypanothione metabolism in trypanosomatid human parasites. Curr. Drug Targets 11(12), 1614-1630 (2010
    • (2010) Curr. Drug Targets , vol.11 , Issue.12 , pp. 1614-1630
    • Olin-Sandoval, V.1    Moreno-Sanchez, R.2    Saavedra, E.3
  • 73
    • 80755142192 scopus 로고    scopus 로고
    • The trypanothione system and the opportunities it offers to create drugs for the neglected kinetoplast diseases
    • Flohe L. The trypanothione system and the opportunities it offers to create drugs for the neglected kinetoplast diseases. Biotechnol. Adv. 30(1), 294-301 (2012
    • (2012) Biotechnol. Adv , vol.30 , Issue.1 , pp. 294-301
    • Flohe, L.1
  • 74
    • 0034697984 scopus 로고    scopus 로고
    • The structure of reduced tryparedoxin peroxidase reveals a decamer and insight into reactivity of 2Cys-peroxiredoxins
    • Alphey MS, Bond CS, Tetaud E, Fairlamb AH, Hunter WN. The structure of reduced tryparedoxin peroxidase reveals a decamer and insight into reactivity of 2Cys-peroxiredoxins. J. Mol. Biol. 300(4), 903-916 (2000
    • (2000) J. Mol. Biol , vol.300 , Issue.4 , pp. 903-916
    • Alphey, M.S.1    Bond, C.S.2    Tetaud, E.3    Fairlamb, A.H.4    Hunter, W.N.5
  • 75
    • 52449084934 scopus 로고    scopus 로고
    • Structural and mechanistic insights into type II trypanosomatid tryparedoxin-dependent peroxidases
    • Alphey MS, Konig J, Fairlamb AH. Structural and mechanistic insights into type II trypanosomatid tryparedoxin-dependent peroxidases. Biochem J. 414(3), 375-381 (2008
    • (2008) Biochem J. , vol.414 , Issue.3 , pp. 375-381
    • Alphey, M.S.1    Konig, J.2    Fairlamb, A.H.3
  • 76
    • 82755171868 scopus 로고    scopus 로고
    • Crystal structure of reduced and of oxidized peroxiredoxin IV enzyme reveals a stable oxidized decamer and a non-disulfide-bonded intermediate in the catalytic cycle
    • Cao Z, Tavender TJ, Roszak AW, Cogdell RJ, Bulleid NJ Crystal structure of reduced and of oxidized peroxiredoxin IV enzyme reveals a stable oxidized decamer and a non-disulfide-bonded intermediate in the catalytic cycle. J. Biol. Chem. 286(49), 42257-42266 (2011
    • (2011) J. Biol. Chem , vol.286 , Issue.49 , pp. 42257-42266
    • Cao, Z.1    Tavender, T.J.2    Roszak, A.W.3    Cogdell, R.J.4    Bulleid, N.J.5
  • 77
    • 84865996192 scopus 로고    scopus 로고
    • The crystal structures of the tryparedoxin-Tryparedoxin peroxidase couple unveil the structural determinants of leishmania detoxification pathway
    • Fiorillo A, Colotti G, Boffi A, Baiocco P, Ilari A. The crystal structures of the tryparedoxin-Tryparedoxin peroxidase couple unveil the structural determinants of Leishmania detoxification pathway. PLoS Negl. Trop. Dis. 6(8), e1781 (2012
    • (2012) PLoS Negl. Trop. Dis , vol.6 , Issue.8
    • Fiorillo, A.1    Colotti, G.2    Boffi, A.3    Baiocco, P.4    Ilari, A.5
  • 78
    • 84055178426 scopus 로고    scopus 로고
    • Structural insights into the peroxidase activity and inactivation of human peroxiredoxin 4
    • Wang X, Wang L, Sun F, Wang CC. Structural insights into the peroxidase activity and inactivation of human peroxiredoxin 4. Biochem. J. 441(1), 113-118 (2012
    • (2012) Biochem. J. , vol.441 , Issue.1 , pp. 113-118
    • Wang, X.1    Wang, L.2    Sun, F.3    Wang, C.C.4
  • 79
    • 0037959650 scopus 로고    scopus 로고
    • Kinetics and redox-sensitive oligomerisation reveal negative subunit cooperativity in tryparedoxin peroxidase of Trypanosoma brucei brucei
    • Budde H, Flohe L, Hecht HJ et al. Kinetics and redox-sensitive oligomerisation reveal negative subunit cooperativity in tryparedoxin peroxidase of Trypanosoma brucei brucei. Biol. Chem. 384(4), 619-633 (2003
    • (2003) Biol. Chem , vol.384 , Issue.4 , pp. 619-633
    • Budde, H.1    Flohe, L.2    Hecht, H.J.3
  • 80
    • 84886544550 scopus 로고    scopus 로고
    • Trypanothione-based redox metabolism of trypanosomatids
    • Jäger T, Koch O, Flohé L (Eds). Wiley-Blackwell Weinheim Germany
    • Comini MA, Flohé L.Trypanothione-based redox metabolism of trypanosomatids. In: Trypanosomatid Diseases. Jäger T, Koch O, Flohé L (Eds). Wiley-Blackwell, Weinheim, Germany, 167-199 (2013
    • (2013) Trypanosomatid Diseases , pp. 167-199
    • Comini, M.A.1    Flohé, L.2
  • 81
    • 84886566871 scopus 로고    scopus 로고
    • Screening approaches towards trypanothione reductase
    • Jäger T, Koch O, Flohé L (Eds). Wiley-Blackwell, Weinheim, Germany
    • Beig M, Oellien F, Krauth-Siegel RL, Selzer PM. Screening approaches towards trypanothione reductase. In: Trypanosomatid Diseases. Jäger T, Koch O, Flohé L (Eds). Wiley-Blackwell, Weinheim, Germany, 385-404 (2013
    • (2013) Trypanosomatid Diseases , pp. 385-404
    • Beig, M.1    Oellien, F.2    Krauth-Siegel, R.L.3    Selzer, P.M.4
  • 82
    • 28544450142 scopus 로고    scopus 로고
    • Irreversible inactivation of trypanothione reductase by unsaturated Mannich bases: A divinyl ketone as key intermediate
    • Lee B, Bauer H, Melchers J et al. Irreversible inactivation of trypanothione reductase by unsaturated Mannich bases: A divinyl ketone as key intermediate. J. Med. Chem. 48, 7400-7410 (2005)
    • (2005) J. Med. Chem , vol.48 , pp. 7400-7410
    • Lee, B.1    Bauer, H.2    Melchers, J.3


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