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Volumn 18, Issue 1, 2011, Pages 113-143

Novel rational drug design strategies with potential to revolutionize malaria chemotherapy

Author keywords

Antimalarial drugs; Apoptosis; Hybrid drugs; Plasmodium falciparum; Prodrugs; Topoisomerases

Indexed keywords

4 AMINOQUINOLINE; ACYL CARRIER PROTEIN; ARTEMETHER PLUS BENFLUMETOL; ARTEMISININ; CAMPTOTHECIN; CASPASE; CASPASE 3; CHLOROQUINE; CLINDAMYCIN; CYCLIN DEPENDENT KINASE; CYSTEINE; DIAMIDINE DERIVATIVE; DIHYDROARTEMISININ; DIHYDROOROTATE DEHYDROGENASE; DNA; FALCIPAIN 2; FATTY ACID SYNTHASE; FERROCHELATASE; GLUTATHIONE; GLUTATHIONE TRANSFERASE; MEFLOQUINE; PEPTIDOMIMETIC AGENT; POTASSIUM ION; PYRAMAX; PYRIMIDINE; REACTIVE OXYGEN METABOLITE; RNA POLYMERASE; SODIUM ION; TUMOR NECROSIS FACTOR ALPHA; UBIQUINONE; UNCLASSIFIED DRUG; UNINDEXED DRUG; UROPORPHYRINOGEN;

EID: 78751550062     PISSN: 09298673     EISSN: None     Source Type: Journal    
DOI: 10.2174/092986711793979742     Document Type: Article
Times cited : (37)

References (383)
  • 1
    • 78751529814 scopus 로고    scopus 로고
    • WHO, 2010. Fact Sheet No. 94 on Malaria, Accessed June, 2010
    • WHO, 2010. Fact Sheet No. 94 on Malaria. http://www.who.int/mediacentre/ factsheets/fs094/en/(Accessed June, 2010).
  • 2
    • 36749000794 scopus 로고    scopus 로고
    • Malaria chemotherapeutics part I: History of antimalarial drug development, currently used therapeutics, and drugs in clinical development
    • Schlitzer, M. Malaria chemotherapeutics part I: History of antimalarial drug development, currently used therapeutics, and drugs in clinical development. Chem. Med. Chem., 2007, 2, 944-986.
    • (2007) Chem. Med. Chem. , vol.2 , pp. 944-986
    • Schlitzer, M.1
  • 3
    • 39449099400 scopus 로고    scopus 로고
    • Plasmodium knowlesi: The fifth human malaria parasite
    • White, N. J. Plasmodium knowlesi: the fifth human malaria parasite. Clin. Infect. Dis., 2008, 46, 172-173.
    • (2008) Clin. Infect. Dis. , vol.46 , pp. 172-173
    • White, N.J.1
  • 6
    • 77949617633 scopus 로고    scopus 로고
    • WHO, Accessed June, 2010
    • WHO, 2009. World Malaria Report 2009. http://www.who.int/malaria/ publications/atoz/9789241563901/en/i ndex.html (Accessed June, 2010).
    • (2009) World Malaria Report 2009
  • 7
    • 14144253009 scopus 로고    scopus 로고
    • Mechanisms of resistance of malaria parasites to antifolates
    • Gregson, A.; Plowe, C. V. Mechanisms of resistance of malaria parasites to antifolates. Pharmacol. Rev., 2005, 57, 117-145.
    • (2005) Pharmacol. Rev. , vol.57 , pp. 117-145
    • Gregson, A.1    Plowe, C.V.2
  • 8
    • 0031852685 scopus 로고    scopus 로고
    • Proteases of malaria parasites: New targets for chemotherapy
    • Rosenthal, P. J. Proteases of malaria parasites: new targets for chemotherapy. Emerg. Infect. Dis., 1998, 4, 49-57.
    • (1998) Emerg. Infect. Dis. , vol.4 , pp. 49-57
    • Rosenthal, P.J.1
  • 9
    • 33751564517 scopus 로고    scopus 로고
    • Design and synthesis of orally active dispiro 1, 2, 4, 5-tetraoxanes; synthetic antimalarials with superior activity to artemisinin
    • Amewu, R.; Stachulski, A. V.; Ward, S. A.; Berry, N. G.; Bray, P. G.; Davies, J.; Labat, G.; Vivas, L.; O'Neill, P. M. Design and synthesis of orally active dispiro 1, 2, 4, 5-tetraoxanes; synthetic antimalarials with superior activity to artemisinin. Org. Biomol. Chem., 2006, 4, 4431-4436.
    • (2006) Org. Biomol. Chem. , vol.4 , pp. 4431-4436
    • Amewu, R.1    Stachulski, A.V.2    Ward, S.A.3    Berry, N.G.4    Bray, P.G.5    Davies, J.6    Labat, G.7    Vivas, L.8    O'Neill, P.M.9
  • 10
    • 0003989708 scopus 로고    scopus 로고
    • Drug Resistance in Malaria. Malaria epidemiology branch, centers for disease control and prevention
    • Bloland, P. B. Drug Resistance in Malaria. Malaria epidemiology branch, centers for disease control and prevention. World Health Organization, 2001, pp. 1-23.
    • (2001) World Health Organization , pp. 1-23
    • Bloland, P.B.1
  • 11
    • 0031847073 scopus 로고    scopus 로고
    • Quinoline antimalarials: Mechanisms of action and resistance and prospects for new agents
    • Foley, M.; Tilley, L. Quinoline antimalarials: mechanisms of action and resistance and prospects for new agents. Pharmacol. Ther., 1998, 79, 55-87.
    • (1998) Pharmacol. Ther. , vol.79 , pp. 55-87
    • Foley, M.1    Tilley, L.2
  • 12
    • 58949085353 scopus 로고    scopus 로고
    • Synthesis and biological evaluation of extraordinarily potent C-10 carba artemisinin dimers against P. falciparum malaria parasites and HL-60 cancer cells
    • Chadwick, J.; Mercer, A. E.; Park, B. K.; Cosstick, R.; O'Neill, P. M. Synthesis and biological evaluation of extraordinarily potent C-10 carba artemisinin dimers against P. falciparum malaria parasites and HL-60 cancer cells. Bioorg. Med. Chem., 2009, 17, 1325-1338.
    • (2009) Bioorg. Med. Chem. , vol.17 , pp. 1325-1338
    • Chadwick, J.1    Mercer, A.E.2    Park, B.K.3    Cosstick, R.4    O'Neill, P.M.5
  • 16
    • 68049146050 scopus 로고    scopus 로고
    • Artemisinin-resistant malaria in Asia
    • Noedl, H.; Socheat, D.; Satimai, W. Artemisinin-resistant malaria in Asia. N. Engl. J. Med., 2009, 361, 540-541.
    • (2009) N. Engl. J. Med. , vol.361 , pp. 540-541
    • Noedl, H.1    Socheat, D.2    Satimai, W.3
  • 17
    • 0242406992 scopus 로고    scopus 로고
    • Antimalarial drug discovery: Old and new approaches
    • Rosenthal, P. J. Antimalarial drug discovery: old and new approaches. J. Exp. Biol., 2003, 206, 3735-3744.
    • (2003) J. Exp. Biol. , vol.206 , pp. 3735-3744
    • Rosenthal, P.J.1
  • 21
    • 0035986688 scopus 로고    scopus 로고
    • Cysteine proteases of malaria parasites: Targets for chemotherapy
    • Rosenthal, P. J.; Sijwali, P. S.; Singh, A.; Shenai, B. R. Cysteine proteases of malaria parasites: targets for chemotherapy. Curr. Pharm. Des., 2002, 8, 1659-1672.
    • (2002) Curr. Pharm. Des. , vol.8 , pp. 1659-1672
    • Rosenthal, P.J.1    Sijwali, P.S.2    Singh, A.3    Shenai, B.R.4
  • 22
    • 0034966663 scopus 로고    scopus 로고
    • Systematic optimization of expression and refolding of the Plasmodium falciparum cysteine protease falcipain-2
    • Sijwali, P. S.; Brinen, L. S.; Rosenthal, P. J. Systematic optimization of expression and refolding of the Plasmodium falciparum cysteine protease falcipain-2. Protein Expr. Purif., 2001, 22, 128-134.
    • (2001) Protein Expr. Purif. , vol.22 , pp. 128-134
    • Sijwali, P.S.1    Brinen, L.S.2    Rosenthal, P.J.3
  • 23
    • 0035644195 scopus 로고    scopus 로고
    • Expression and characterization of the Plasmodium falciparum haemoglobinase falcipain-3
    • Sijwali, P. S.; Shenai, B. R.; Gut, J.; Singh, A.; Rosenthal, P. J. Expression and characterization of the Plasmodium falciparum haemoglobinase falcipain-3. Biochem. J., 2001, 360, 481-489.
    • (2001) Biochem. J. , vol.360 , pp. 481-489
    • Sijwali, P.S.1    Shenai, B.R.2    Gut, J.3    Singh, A.4    Rosenthal, P.J.5
  • 25
    • 0033057631 scopus 로고    scopus 로고
    • Antimalarial effects in mice of orally administered peptidyl cysteine protease inhibitors
    • Olson, J. E.; Lee, G. K.; Semenov, A.; Rosenthal, P. J. Antimalarial effects in mice of orally administered peptidyl cysteine protease inhibitors. Bioorg. Med. Chem., 1999, 7, 633-638.
    • (1999) Bioorg. Med. Chem. , vol.7 , pp. 633-638
    • Olson, J.E.1    Lee, G.K.2    Semenov, A.3    Rosenthal, P.J.4
  • 26
    • 35648986600 scopus 로고    scopus 로고
    • Design, synthesis, and antimalarial activity of structural chimeras of thiosemicarbazone and ferroquine analogues
    • Biot, C.; Pradines, B.; Sergeant, M. H.; Gut, J.; Rosenthal, P. J.; Chibale, K. Design, synthesis, and antimalarial activity of structural chimeras of thiosemicarbazone and ferroquine analogues. Bioorg Med. Chem. Lett., 2007, 17, 6434-6438.
    • (2007) Bioorg Med. Chem. Lett. , vol.17 , pp. 6434-6438
    • Biot, C.1    Pradines, B.2    Sergeant, M.H.3    Gut, J.4    Rosenthal, P.J.5    Chibale, K.6
  • 27
    • 77952715810 scopus 로고    scopus 로고
    • Mechanism-based inhibitors of the aspartyl protease plasmepsin II as potential antimalarial agents
    • Gupta, D.; Yedidi, R. S.; Varghese, S.; Kovari, L. C.; Woster, P. M. Mechanism-based inhibitors of the aspartyl protease plasmepsin II as potential antimalarial agents. J. Med. Chem., 2010, 53, 4234-4247.
    • (2010) J. Med. Chem. , vol.53 , pp. 4234-4247
    • Gupta, D.1    Yedidi, R.S.2    Varghese, S.3    Kovari, L.C.4    Woster, P.M.5
  • 29
    • 77953773127 scopus 로고    scopus 로고
    • Plasmodium dihydroorotate dehydrogenase: A promising target for novel anti-malarial chemotherapy
    • Phillips, M. A.; Rathod, P. K. Plasmodium dihydroorotate dehydrogenase: a promising target for novel anti-malarial chemotherapy. Infect. Disord. Drug Targets, 2010, 10, 226-239.
    • (2010) Infect. Disord. Drug Targets , vol.10 , pp. 226-239
    • Phillips, M.A.1    Rathod, P.K.2
  • 32
    • 0031466305 scopus 로고    scopus 로고
    • Cyclin-dependent kinases: Engines, clocks, and microprocessors
    • Morgan, D. O. Cyclin-dependent kinases: engines, clocks, and microprocessors. Annu. Rev. Cell Dev. Biol., 1997, 13, 261-291.
    • (1997) Annu. Rev. Cell. Dev. Biol. , vol.13 , pp. 261-291
    • Morgan, D.O.1
  • 33
    • 12744281184 scopus 로고    scopus 로고
    • Rational inhibitor design and iterative screening in the identification of selective plasmodial cyclin dependent kinase inhibitors
    • Keenan, S. M.; Geyer, J. A.; Welsh, W. J.; Prigge, S. T.; Waters, N. C. Rational inhibitor design and iterative screening in the identification of selective plasmodial cyclin dependent kinase inhibitors. Comb. Chem. High Throughput Screen., 2005, 8, 27-38.
    • (2005) Comb. Chem. High Throughput Screen. , vol.8 , pp. 27-38
    • Keenan, S.M.1    Geyer, J.A.2    Welsh, W.J.3    Prigge, S.T.4    Waters, N.C.5
  • 34
    • 0037312866 scopus 로고    scopus 로고
    • Cyclin-dependent protein kinases as therapeutic drug targets for antimalarial drug development
    • Waters, N. C.; Geyer, J. A. Cyclin-dependent protein kinases as therapeutic drug targets for antimalarial drug development. Expert Opin. Ther. Targets, 2003, 7, 7-17.
    • (2003) Expert Opin. Ther. Targets , vol.7 , pp. 7-17
    • Waters, N.C.1    Geyer, J.A.2
  • 35
    • 0029418115 scopus 로고
    • The regulation and functions of cdk7
    • Shuttleworth, J. The regulation and functions of cdk7. Prog. Cell Cycle Res., 1995, 1, 229-240.
    • (1995) Prog. Cell. Cycle Res. , vol.1 , pp. 229-240
    • Shuttleworth, J.1
  • 36
    • 7644221040 scopus 로고    scopus 로고
    • Export of Plasmodium falciparum calciumdependent protein kinase 1 to the parasitophorous vacuole is dependent on three N-terminal membrane anchor motifs
    • Moskes, C.; Burghaus, P. A.; Wernli, B.; Sauder, U.; Durrenberger, M.; Kappes, B. Export of Plasmodium falciparum calciumdependent protein kinase 1 to the parasitophorous vacuole is dependent on three N-terminal membrane anchor motifs. Mol. Microbiol., 2004, 54, 676-691.
    • (2004) Mol. Microbiol. , vol.54 , pp. 676-691
    • Moskes, C.1    Burghaus, P.A.2    Wernli, B.3    Sauder, U.4    Durrenberger, M.5    Kappes, B.6
  • 37
    • 0142025055 scopus 로고    scopus 로고
    • Calcium-regulated protein kinases of plants
    • Harmon, A. C. Calcium-regulated protein kinases of plants. Gravit. Space Biol. Bull., 2003, 16, 83-90.
    • (2003) Gravit. Space Biol. Bull. , vol.16 , pp. 83-90
    • Harmon, A.C.1
  • 38
    • 0033231908 scopus 로고    scopus 로고
    • An overview of Plasmodium protein kinases
    • Kappes, B.; Doerig, C. D.; Graeser, R. An overview of Plasmodium protein kinases. Parasitol. Today, 1999, 15, 449-454.
    • (1999) Parasitol. Today , vol.15 , pp. 449-454
    • Kappes, B.1    Doerig, C.D.2    Graeser, R.3
  • 39
    • 0030806327 scopus 로고    scopus 로고
    • Molecular cloning and characterization of a second calcium-dependent protein kinase of Plasmodium falciparum
    • DOI 10.1016/S0166-6851(97)00052-2, PII S0166685197000522
    • Farber, P. M.; Graeser, R.; Franklin, R. M.; Kappes, B. Molecular cloning and characterization of a second calcium-dependent protein kinase of Plasmodium falciparum. Mol. Biochem. Parasitol., 1997, 87, 211-216. (Pubitemid 27283283)
    • (1997) Molecular and Biochemical Parasitology , vol.87 , Issue.2 , pp. 211-216
    • Farber, P.M.1    Graeser, R.2    Franklin, R.M.3    Kappes, B.4
  • 40
    • 2342611064 scopus 로고    scopus 로고
    • Calcium and a calcium-dependent protein kinase regulate gamete formation and mosquito transmission in a malaria parasite
    • Billker, O.; Dechamps, S.; Tewari, R.; Wenig, G.; Franke-Fayard, B.; Brinkmann, V. Calcium and a calcium-dependent protein kinase regulate gamete formation and mosquito transmission in a malaria parasite. Cell, 2004, 117, 503-514.
    • (2004) Cell. , vol.117 , pp. 503-514
    • Billker, O.1    Dechamps, S.2    Tewari, R.3    Wenig, G.4    Franke-Fayard, B.5    Brinkmann, V.6
  • 43
    • 0029130017 scopus 로고
    • Plasmodium berghei: Implication of intracellular glutathione and its related enzyme in chloroquine resistance in vivo
    • Dubois, V. L.; Platel, D. F.; Pauly, G.; Tribouley-Duret, J. Plasmodium berghei: implication of intracellular glutathione and its related enzyme in chloroquine resistance in vivo. Exp. Parasitol., 1995, 81, 117-124.
    • (1995) Exp. Parasitol. , vol.81 , pp. 117-124
    • Dubois, V.L.1    Platel, D.F.2    Pauly, G.3    Tribouley-Duret, J.4
  • 44
    • 0033168578 scopus 로고    scopus 로고
    • Kinetics of inhibition of glutathione-mediated degradation of ferriprotoporphyrin IX by antimalarial drugs
    • Famin, O.; Krugliak, M.; Ginsburg, H. Kinetics of inhibition of glutathione-mediated degradation of ferriprotoporphyrin IX by antimalarial drugs. Biochem. Pharmacol., 1999, 58, 59-68.
    • (1999) Biochem. Pharmacol. , vol.58 , pp. 59-68
    • Famin, O.1    Krugliak, M.2    Ginsburg, H.3
  • 45
    • 0032781364 scopus 로고    scopus 로고
    • Resistance mutations reveal the atovaquone-binding domain of cytochrome b in malaria parasites
    • Srivastava, I. K.; Morrisey, J. M.; Darrouzet, E.; Daldal, F.; Vaidya, A. B. Resistance mutations reveal the atovaquone-binding domain of cytochrome b in malaria parasites. Mol. Microbiol., 1999, 33, 704-711.
    • (1999) Mol. Microbiol. , vol.33 , pp. 704-711
    • Srivastava, I.K.1    Morrisey, J.M.2    Darrouzet, E.3    Daldal, F.4    Vaidya, A.B.5
  • 46
    • 34250624067 scopus 로고    scopus 로고
    • Effect of Plasmodium yoelii nigeriensis infection on hepatic and splenic glutathione-S-transferase (s) in Swiss albino and db/+ mice: Efficacy of mefloquine and menadione in antimalarial chemotherapy
    • Ahmad, R.; Srivastava, A. K. Effect of Plasmodium yoelii nigeriensis infection on hepatic and splenic glutathione-S-transferase (s) in Swiss albino and db/+ mice: efficacy of mefloquine and menadione in antimalarial chemotherapy. Parasitology, 2007, 134, 931-938.
    • (2007) Parasitology , vol.134 , pp. 931-938
    • Ahmad, R.1    Srivastava, A.K.2
  • 47
    • 0029266564 scopus 로고
    • Potential contribution of the glutathione S-transferase supergene family to resistance to oxidative stress
    • Hayes, J. D.; Strange, R. C. Potential contribution of the glutathione S-transferase supergene family to resistance to oxidative stress. Free Radic. Res., 1995, 22, 193-207.
    • (1995) Free Radic. Res. , vol.22 , pp. 193-207
    • Hayes, J.D.1    Strange, R.C.2
  • 48
    • 0032815207 scopus 로고    scopus 로고
    • Apicomplexan plastids as drug targets
    • McFadden, G. I.; Roos, D. S. Apicomplexan plastids as drug targets. Trends Microbiol., 1999, 7, 328-333.
    • (1999) Trends Microbiol. , vol.7 , pp. 328-333
    • McFadden, G.I.1    Roos, D.S.2
  • 49
    • 34249986680 scopus 로고    scopus 로고
    • Nuclear gyrB encodes a functional subunit of the Plasmodium falciparum gyrase that is involved in apicoplast DNA replication
    • Raghu Ram, E. V.; Kumar, A.; Biswas, S.; Kumar, A.; Chaubey, S.; Siddiqi, M. I.; Habib, S. Nuclear gyrB encodes a functional subunit of the Plasmodium falciparum gyrase that is involved in apicoplast DNA replication. Mol. Biochem. Parasitol., 2007, 154, 30-39.
    • (2007) Mol. Biochem. Parasitol. , vol.154 , pp. 30-39
    • Raghu Ram, E.V.1    Kumar, A.2    Biswas, S.3    Kumar, A.4    Chaubey, S.5    Siddiqi, M.I.6    Habib, S.7
  • 51
    • 0030011405 scopus 로고    scopus 로고
    • Recent advances in the biosynthesis of plant fatty acids
    • Harwood, J. L. Recent advances in the biosynthesis of plant fatty acids. Biochim. Biophys. Acta, 1996, 1301, 7-56.
    • (1996) Biochim. Biophys. Acta , vol.1301 , pp. 7-56
    • Harwood, J.L.1
  • 54
    • 0035126479 scopus 로고    scopus 로고
    • Triclosan offers protection against blood stages of malaria by inhibiting enoyl-ACP reductase of Plasmodium falciparum
    • Surolia, N.; Surolia, A. Triclosan offers protection against blood stages of malaria by inhibiting enoyl-ACP reductase of Plasmodium falciparum. Nat. Med., 2001, 7, 167-173.
    • (2001) Nat. Med. , vol.7 , pp. 167-173
    • Surolia, N.1    Surolia, A.2
  • 55
    • 0034780806 scopus 로고    scopus 로고
    • Bacterial fatty acid biosynthesis: Targets for antibacterial drug discovery
    • Campbell, J. W.; Cronan, J. E., Jr. Bacterial fatty acid biosynthesis: targets for antibacterial drug discovery. Annu. Rev. Microbiol., 2001, 55, 305-332.
    • (2001) Annu. Rev. Microbiol. , vol.55 , pp. 305-332
    • Campbell, J.W.1    Cronan Jr., J.E.2
  • 57
    • 0037066782 scopus 로고    scopus 로고
    • Structural elucidation of the specificity of the antibacterial agent triclosan for malarial enoyl acyl carrier protein reductase
    • Perozzo, R.; Kuo, M.; Sidhu, A. S.; Valiyaveettil, J. T.; Bittman, R.; Jacobs, W. R., Jr.; Fidock, D. A.; Sacchettini, J. C. Structural elucidation of the specificity of the antibacterial agent triclosan for malarial enoyl acyl carrier protein reductase. J. Biol. Chem., 2002, 277, 13106-13114.
    • (2002) J. Biol. Chem. , vol.277 , pp. 13106-13114
    • Perozzo, R.1    Kuo, M.2    Sidhu, A.S.3    Valiyaveettil, J.T.4    Bittman, R.5    Jacobs Jr., W.R.6    Fidock, D.A.7    Sacchettini, J.C.8
  • 60
    • 13444301270 scopus 로고    scopus 로고
    • Parasite plastids: Approaching the endgame
    • Wilson, R. J. M. Parasite plastids: approaching the endgame. Biol. Rev., 2005, 80, 129-153.
    • (2005) Biol. Rev. , vol.80 , pp. 129-153
    • Wilson, R.J.M.1
  • 63
    • 0037625396 scopus 로고    scopus 로고
    • Fosmidomycin for the treatment of malaria
    • Wiesner, J.; Borrmann, S.; Jomaa, H. Fosmidomycin for the treatment of malaria. Parasitol. Res., 2003, 90 Suppl 2, S71-76.
    • (2003) Parasitol. Res. , vol.90 , Issue.2 SUPPL.
    • Wiesner, J.1    Borrmann, S.2    Jomaa, H.3
  • 64
    • 0026785410 scopus 로고
    • De novo biosynthesis of heme offers a new chemotherapeutic target in the human malarial parasite
    • Surolia, N.; Padmanaban, G. de novo biosynthesis of heme offers a new chemotherapeutic target in the human malarial parasite. Biochem. Biophys. Res. Commun., 1992, 187, 744-750.
    • (1992) Biochem. Biophys. Res. Commun. , vol.187 , pp. 744-750
    • Surolia, N.1    Padmanaban, G.2
  • 65
    • 0033834719 scopus 로고    scopus 로고
    • Import of host delta-aminolevulinate dehydratase into the malarial parasite: Identification of a new drug target
    • Bonday, Z. Q.; Dhanasekaran, S.; Rangarajan, P. N.; Padmanaban, G. Import of host delta-aminolevulinate dehydratase into the malarial parasite: identification of a new drug target. Nat. Med., 2000, 6, 898-903.
    • (2000) Nat. Med. , vol.6 , pp. 898-903
    • Bonday, Z.Q.1    Dhanasekaran, S.2    Rangarajan, P.N.3    Padmanaban, G.4
  • 67
    • 0036230756 scopus 로고    scopus 로고
    • The genome of Plasmodium falciparum encodes an active delta-aminolevulinic acid dehydratase
    • Sato, S.; Wilson, R. J. The genome of Plasmodium falciparum encodes an active delta-aminolevulinic acid dehydratase. Curr. Genet., 2002, 40, 391-398.
    • (2002) Curr. Genet. , vol.40 , pp. 391-398
    • Sato, S.1    Wilson, R.J.2
  • 68
    • 0037189526 scopus 로고    scopus 로고
    • Processing of an apicoplast leader sequence in Plasmodium falciparum and the identification of a putative leader cleavage enzyme
    • van Dooren, G. G.; Su, V.; D'Ombrain, M. C.; McFadden, G. I. Processing of an apicoplast leader sequence in Plasmodium falciparum and the identification of a putative leader cleavage enzyme. J. Biol. Chem., 2002, 277, 23612-23619.
    • (2002) J. Biol. Chem. , vol.277 , pp. 23612-23619
    • Van Dooren, G.G.1    Su, V.2    D'Ombrain, M.C.3    McFadden, G.I.4
  • 69
    • 0037108901 scopus 로고    scopus 로고
    • Involvement of delta-aminolaevulinate synthase encoded by the parasite gene in de novo haem synthesis by Plasmodium falciparum
    • Varadharajan, S.; Dhanasekaran, S.; Bonday, Z. Q.; Rangarajan, P. N.; Padmanaban, G. Involvement of delta-aminolaevulinate synthase encoded by the parasite gene in de novo haem synthesis by Plasmodium falciparum. Biochem. J., 2002, 367, 321-327.
    • (2002) Biochem. J. , vol.367 , pp. 321-327
    • Varadharajan, S.1    Dhanasekaran, S.2    Bonday, Z.Q.3    Rangarajan, P.N.4    Padmanaban, G.5
  • 71
    • 1942444611 scopus 로고    scopus 로고
    • Enzymes for heme biosynthesis are found in both the mitochondrion and plastid of the malaria parasite Plasmodium falciparum
    • Sato, S.; Clough, B.; Coates, L.; Wilson, R. J. Enzymes for heme biosynthesis are found in both the mitochondrion and plastid of the malaria parasite Plasmodium falciparum. Protist, 2004, 155, 117-125.
    • (2004) Protist , vol.155 , pp. 117-125
    • Sato, S.1    Clough, B.2    Coates, L.3    Wilson, R.J.4
  • 72
    • 0029034851 scopus 로고
    • Plasmodium falciparum: Alterations in organelle transcript abundance during the erythrocytic cycle
    • Feagin, J. E.; Drew, M. E. Plasmodium falciparum: alterations in organelle transcript abundance during the erythrocytic cycle. Exp. Parasitol., 1995, 80, 430-440.
    • (1995) Exp. Parasitol. , vol.80 , pp. 430-440
    • Feagin, J.E.1    Drew, M.E.2
  • 73
    • 0030179502 scopus 로고    scopus 로고
    • Characterization of the delta-aminolevulinate synthase gene homologue in P
    • Wilson, C. M.; Smith, A. B.; Baylon, R. V. Characterization of the delta-aminolevulinate synthase gene homologue in P. falciparum. Mol. Biochem. Parasitol., 1996, 79, 135-140.
    • (1996) Falciparum. Mol. Biochem. Parasitol. , vol.79 , pp. 135-140
    • Wilson, C.M.1    Smith, A.B.2    Baylon, R.V.3
  • 75
    • 0033180232 scopus 로고    scopus 로고
    • Antibiotic inhibitors of organellar protein synthesis in Plasmodium falciparum
    • Clough, B.; Rangachari, K.; Strath, M.; Preiser, P. R.; Wilson, R. J. Antibiotic inhibitors of organellar protein synthesis in Plasmodium falciparum. Protist, 1999, 150, 189-195.
    • (1999) Protist , vol.150 , pp. 189-195
    • Clough, B.1    Rangachari, K.2    Strath, M.3    Preiser, P.R.4    Wilson, R.J.5
  • 76
    • 0033180525 scopus 로고    scopus 로고
    • Protein synthesis in the plastid of Plasmodium falciparum
    • Roy, A.; Cox, R. A.; Williamson, D. H.; Wilson, R. J. Protein synthesis in the plastid of Plasmodium falciparum. Protist, 1999, 150, 183-188.
    • (1999) Protist , vol.150 , pp. 183-188
    • Roy, A.1    Cox, R.A.2    Williamson, D.H.3    Wilson, R.J.4
  • 78
    • 0030008510 scopus 로고    scopus 로고
    • Stagespecific processing of Pfs230, a Plasmodium falciparum transmission-blocking vaccine candidate
    • Williamson, K. C.; Fujioka, H.; Aikawa, M.; Kaslow, D. C. Stagespecific processing of Pfs230, a Plasmodium falciparum transmission-blocking vaccine candidate. Mol. Biochem. Parasitol., 1996, 78, 161-169.
    • (1996) Mol. Biochem. Parasitol. , vol.78 , pp. 161-169
    • Williamson, K.C.1    Fujioka, H.2    Aikawa, M.3    Kaslow, D.C.4
  • 79
    • 0023686315 scopus 로고
    • Activity of fluoroquinolone antibiotics against Plasmodium falciparum in vitro
    • Divo, A. A.; Sartorelli, A. C.; Patton, C. L.; Bia, F. J. Activity of fluoroquinolone antibiotics against Plasmodium falciparum in vitro. Antimicrob. Agents Chemother., 1988, 32, 1182-1186.
    • (1988) Antimicrob. Agents Chemother. , vol.32 , pp. 1182-1186
    • Divo, A.A.1    Sartorelli, A.C.2    Patton, C.L.3    Bia, F.J.4
  • 80
    • 0031431683 scopus 로고    scopus 로고
    • Topoisomerase II inhibitors induce cleavage of nuclear and 35-kb plastid DNAs in the malarial parasite Plasmodium falciparum
    • Weissig, V.; Vetro-Widenhouse, T. S.; Rowe, T. C. Topoisomerase II inhibitors induce cleavage of nuclear and 35-kb plastid DNAs in the malarial parasite Plasmodium falciparum. DNA Cell Biol., 1997, 16, 1483-1492.
    • (1997) DNA Cell. Biol. , vol.16 , pp. 1483-1492
    • Weissig, V.1    Vetro-Widenhouse, T.S.2    Rowe, T.C.3
  • 81
    • 0031444101 scopus 로고    scopus 로고
    • A plastid organelle as a drug target in apicomplexan parasites
    • Fichera, M. E.; Roos, D. S. A plastid organelle as a drug target in apicomplexan parasites. Nature, 1997, 390, 407-409.
    • (1997) Nature , vol.390 , pp. 407-409
    • Fichera, M.E.1    Roos, D.S.2
  • 82
    • 0036065460 scopus 로고    scopus 로고
    • The plastid DNA of the malaria parasite Plasmodium falciparum is replicated by two mechanisms
    • Williamson, D. H.; Preiser, P. R.; Moore, P. W.; McCready, S.; Strath, M.; Wilson, R. J. The plastid DNA of the malaria parasite Plasmodium falciparum is replicated by two mechanisms. Mol. Microbiol., 2002, 45, 533-542.
    • (2002) Mol. Microbiol. , vol.45 , pp. 533-542
    • Williamson, D.H.1    Preiser, P.R.2    Moore, P.W.3    McCready, S.4    Strath, M.5    Wilson, R.J.6
  • 83
    • 0032742420 scopus 로고    scopus 로고
    • Malarial genome comes into view
    • 1265
    • Pennisi, E. Malarial genome comes into view. Science, 1999, 286, 1263;1265.
    • (1999) Science , vol.286 , pp. 1263
    • Pennisi, E.1
  • 84
    • 33947638347 scopus 로고    scopus 로고
    • Molecular cloning of apicoplast-targeted Plasmodium falciparum DNA gyrase genes: Unique intrinsic ATPase activity and ATP-independent dimerization of PfGyrB subunit
    • Dar, M. A.; Sharma, A.; Mondal, N.; Dhar, S. K. Molecular cloning of apicoplast-targeted Plasmodium falciparum DNA gyrase genes: unique intrinsic ATPase activity and ATP-independent dimerization of PfGyrB subunit. Eukaryot. Cell., 2007, 6, 398-412.
    • (2007) Eukaryot. Cell. , vol.6 , pp. 398-412
    • Dar, M.A.1    Sharma, A.2    Mondal, N.3    Dhar, S.K.4
  • 85
    • 0027419771 scopus 로고
    • The 43-kilodalton N-terminal fragment of the DNA gyrase B protein hydrolyzes ATP and binds coumarin drugs
    • Ali, J. A.; Jackson, A. P.; Howells, A. J.; Maxwell, A. The 43-kilodalton N-terminal fragment of the DNA gyrase B protein hydrolyzes ATP and binds coumarin drugs. Biochemistry, 1993, 32, 2717-2724.
    • (1993) Biochemistry , vol.32 , pp. 2717-2724
    • Ali, J.A.1    Jackson, A.P.2    Howells, A.J.3    Maxwell, A.4
  • 86
    • 34948847580 scopus 로고    scopus 로고
    • Multiple antibiotics exert delayed effects against the Plasmodium falciparum apicoplast
    • Dahl, E. L.; Rosenthal, P. J. Multiple antibiotics exert delayed effects against the Plasmodium falciparum apicoplast. Antimicrob. Agents Chemother., 2007, 51, 3485-3490.
    • (2007) Antimicrob. Agents Chemother. , vol.51 , pp. 3485-3490
    • Dahl, E.L.1    Rosenthal, P.J.2
  • 87
    • 13444291112 scopus 로고    scopus 로고
    • Expression and characterization of the ATP-binding domain of a malarial Plasmodium vivax gene homologous to the B-subunit of the bacterial topoisomerase DNA gyrase
    • Khor, V.; Yowell, C.; Dame, J. B.; Rowe, T. C. Expression and characterization of the ATP-binding domain of a malarial Plasmodium vivax gene homologous to the B-subunit of the bacterial topoisomerase DNA gyrase. Mol. Biochem. Parasitol., 2005, 140, 107-117.
    • (2005) Mol. Biochem. Parasitol. , vol.140 , pp. 107-117
    • Khor, V.1    Yowell, C.2    Dame, J.B.3    Rowe, T.C.4
  • 90
    • 0038304827 scopus 로고    scopus 로고
    • Apicomplexan parasites contain a single lipoic acid synthase located in the plastid
    • Thomsen-Zieger, N.; Schachtner, J.; Seeber, F. Apicomplexan parasites contain a single lipoic acid synthase located in the plastid. FEBS Lett., 2003, 547, 80-86.
    • (2003) FEBS Lett. , vol.547 , pp. 80-86
    • Thomsen-Zieger, N.1    Schachtner, J.2    Seeber, F.3
  • 91
    • 27844559736 scopus 로고    scopus 로고
    • Plasmodium falciparum possesses organelle-specific alpha-keto acid dehydrogenase complexes and lipoylation pathways
    • Gunther, S.; McMillan, P. J.; Wallace, L. J.; Muller, S. Plasmodium falciparum possesses organelle-specific alpha-keto acid dehydrogenase complexes and lipoylation pathways. Biochem. Soc. Trans., 2005, 33, 977-980.
    • (2005) Biochem. Soc. Trans. , vol.33 , pp. 977-980
    • Gunther, S.1    McMillan, P.J.2    Wallace, L.J.3    Muller, S.4
  • 92
    • 33847398001 scopus 로고    scopus 로고
    • Specific role of mitochondrial electron transport in blood-stage Plasmodium falciparum
    • Painter, H. J.; Morrisey, J. M.; Mather, M. W.; Vaidya, A. B. Specific role of mitochondrial electron transport in blood-stage Plasmodium falciparum. Nature, 2007, 446, 88-91.
    • (2007) Nature , vol.446 , pp. 88-91
    • Painter, H.J.1    Morrisey, J.M.2    Mather, M.W.3    Vaidya, A.B.4
  • 93
    • 0031052025 scopus 로고    scopus 로고
    • Atovaquone, a broad spectrum antiparasitic drug, collapses mitochondrial membrane potential in a malarial parasite
    • Srivastava, I. K.; Rottenberg, H.; Vaidya, A. B. Atovaquone, a broad spectrum antiparasitic drug, collapses mitochondrial membrane potential in a malarial parasite. J. Biol. Chem., 1997, 272, 3961-3966.
    • (1997) J. Biol. Chem. , vol.272 , pp. 3961-3966
    • Srivastava, I.K.1    Rottenberg, H.2    Vaidya, A.B.3
  • 96
    • 1942447877 scopus 로고    scopus 로고
    • The cytochrome bc1 complex: Function in the context of structure
    • Crofts, A. R. The cytochrome bc1 complex: function in the context of structure. Annu. Rev. Physiol., 2004, 66, 689-733.
    • (2004) Annu. Rev. Physiol. , vol.66 , pp. 689-733
    • Crofts, A.R.1
  • 98
    • 37249080857 scopus 로고    scopus 로고
    • Malaria: Differential parasite drive
    • van Dooren, G. G.; McFadden, G. I. Malaria: differential parasite drive. Nature, 2007, 450, 955-956.
    • (2007) Nature , vol.450 , pp. 955-956
    • Van Dooren, G.G.1    McFadden, G.I.2
  • 99
    • 62149090637 scopus 로고    scopus 로고
    • Semi-synthetic and synthetic 1, 2, 4-trioxaquines and 1, 2, 4-trioxolaquines: Synthesis, preliminary SAR and comparison with acridine endoperoxide conjugates
    • Araujo, N. C.; Barton, V.; Jones, M.; Stocks, P. A.; Ward, S. A.; Davies, J.; Bray, P. G.; Shone, A. E.; Cristiano, M. L.; O'Neill, P. M. Semi-synthetic and synthetic 1, 2, 4-trioxaquines and 1, 2, 4-trioxolaquines: synthesis, preliminary SAR and comparison with acridine endoperoxide conjugates. Bioorg. Med. Chem. Lett., 2009, 19, 2038-2043.
    • (2009) Bioorg. Med. Chem. Lett. , vol.19 , pp. 2038-2043
    • Araujo, N.C.1    Barton, V.2    Jones, M.3    Stocks, P.A.4    Ward, S.A.5    Davies, J.6    Bray, P.G.7    Shone, A.E.8    Cristiano, M.L.9    O'Neill, P.M.10
  • 100
    • 0030757751 scopus 로고    scopus 로고
    • Morphological and biochemical characterization and analysis of apoptosis
    • Allen, R. T.; Hunter, W. J., 3rd; Agrawal, D. K. Morphological and biochemical characterization and analysis of apoptosis. J. Pharmacol. Toxicol. Methods, 1997, 37, 215-228.
    • (1997) J. Pharmacol. Toxicol. Methods , vol.37 , pp. 215-228
    • Allen, R.T.1    Hunter III, W.J.2    Agrawal, D.K.3
  • 101
    • 3042801604 scopus 로고    scopus 로고
    • Morphological features of cell death
    • Ziegler, U.; Groscurth, P. Morphological features of cell death. News Physiol. Sci., 2004, 19, 124-128.
    • (2004) News Physiol. Sci. , vol.19 , pp. 124-128
    • Ziegler, U.1    Groscurth, P.2
  • 104
    • 1642473938 scopus 로고    scopus 로고
    • Metronidazole induces programmed cell death in the protozoan parasite Blastocystis hominis
    • Nasirudeen, A. M.; Hian, Y. E.; Singh, M.; Tan, K. S. Metronidazole induces programmed cell death in the protozoan parasite Blastocystis hominis. Microbiology, 2004, 150, 33-43.
    • (2004) Microbiology , vol.150 , pp. 33-43
    • Nasirudeen, A.M.1    Hian, Y.E.2    Singh, M.3    Tan, K.S.4
  • 105
    • 36448964485 scopus 로고    scopus 로고
    • Programmed cell death in Entamoeba histolytica induced by the aminoglycoside G418
    • DOI 10.1099/mic.0.2007/008599-0
    • Villalba, J. D.; Gomez, C.; Medel, O.; Sanchez, V.; Carrero, J. C.; Shibayama, M.; Ishiwara, D. G. Programmed cell death in Entamoeba histolytica induced by the aminoglycoside G418. Microbiology, 2007, 153, 3852-3863. (Pubitemid 350168264)
    • (2007) Microbiology , vol.153 , Issue.11 , pp. 3852-3863
    • Villalba, J.D'A.1    Gomez, C.2    Medel, O.3    Sanchez, V.4    Carrero, J.C.5    Shibayama, M.6    Perez Ishiwara, D.G.7
  • 106
    • 0031846964 scopus 로고    scopus 로고
    • Intercomparison of apoptosis morphology with active DNA cleavage on single cells in vitro and on testis tumours
    • Abend, M.; Schmelz, H. U.; Kraft, K.; Rhein, A. P.; van Beuningen, D.; Sparwasser, C. Intercomparison of apoptosis morphology with active DNA cleavage on single cells in vitro and on testis tumours. J. Pathol., 1998, 185, 419-426.
    • (1998) J. Pathol. , vol.185 , pp. 419-426
    • Abend, M.1    Schmelz, H.U.2    Kraft, K.3    Rhein, A.P.4    Van Beuningen, D.5    Sparwasser, C.6
  • 107
    • 0032852196 scopus 로고    scopus 로고
    • Modified approach for apoptosis detection reveals changes in apoptotic processes in the seminoma-associated tissue
    • Abend, M.; Schmelz, H. U.; Kraft, K.; van Beuningen, D.; Sparwasser, C. Modified approach for apoptosis detection reveals changes in apoptotic processes in the seminoma-associated tissue. Apoptosis, 1999, 4, 283-290.
    • (1999) Apoptosis , vol.4 , pp. 283-290
    • Abend, M.1    Schmelz, H.U.2    Kraft, K.3    Van Beuningen, D.4    Sparwasser, C.5
  • 109
    • 3142686069 scopus 로고    scopus 로고
    • Programmed cell death in trypanosomatids: A way to maximize their biological fitness?
    • Nguewa, P. A.; Fuertes, M. A.; Valladares, B.; Alonso, C.; Perez, J. M. Programmed cell death in trypanosomatids: a way to maximize their biological fitness? Trends Parasitol., 2004, 20, 375-380.
    • (2004) Trends Parasitol. , vol.20 , pp. 375-380
    • Nguewa, P.A.1    Fuertes, M.A.2    Valladares, B.3    Alonso, C.4    Perez, J.M.5
  • 110
    • 0036792472 scopus 로고    scopus 로고
    • Cell death in Leishmania induced by stress and differentiation: Programmed cell death or necrosis?
    • Zangger, H.; Mottram, J. C.; Fasel, N. Cell death in Leishmania induced by stress and differentiation: programmed cell death or necrosis? Cell Death Differ., 2002, 9, 1126-1139.
    • (2002) Cell. Death Differ. , vol.9 , pp. 1126-1139
    • Zangger, H.1    Mottram, J.C.2    Fasel, N.3
  • 111
    • 0033638182 scopus 로고    scopus 로고
    • Identification of paracaspases and metacaspases: Two ancient families of caspase-like proteins, one of which plays a key role in MALT lymphoma
    • Uren, A. G.; O'Rourke, K.; Aravind, L. A.; Pisabarro, M. T.; Seshagiri, S.; Koonin, E. V.; Dixit, V. M. Identification of paracaspases and metacaspases: two ancient families of caspase-like proteins, one of which plays a key role in MALT lymphoma. Mol. Cell., 2000, 6, 961-967.
    • (2000) Mol. Cell. , vol.6 , pp. 961-967
    • Uren, A.G.1    O'Rourke, K.2    Aravind, L.A.3    Pisabarro, M.T.4    Seshagiri, S.5    Koonin, E.V.6    Dixit, V.M.7
  • 113
    • 33746154897 scopus 로고    scopus 로고
    • Poly (ADP-ribose) polymerase-1 inhibitor 3-aminobenzamide enhances apoptosis induction by platinum complexes in cisplatin-resistant tumor cells
    • Nguewa, P. A.; Fuertes, M. A.; Cepeda, V.; Alonso, C.; Quevedo, C.; Soto, M.; Perez, J. M. Poly (ADP-ribose) polymerase-1 inhibitor 3-aminobenzamide enhances apoptosis induction by platinum complexes in cisplatin-resistant tumor cells. Med. Chem., 2006, 2, 47-53.
    • (2006) Med. Chem. , vol.2 , pp. 47-53
    • Nguewa, P.A.1    Fuertes, M.A.2    Cepeda, V.3    Alonso, C.4    Quevedo, C.5    Soto, M.6    Perez, J.M.7
  • 114
    • 0036081335 scopus 로고    scopus 로고
    • Nitric oxide-mediated proteasome-dependent oligonucleosomal DNA fragmentation in Leishmania amazonensis amastigotes
    • Holzmuller, P.; Sereno, D.; Cavaleyra, M.; Mangot, I.; Daulouede, S.; Vincendeau, P.; Lemesre, J. L. Nitric oxide-mediated proteasome-dependent oligonucleosomal DNA fragmentation in Leishmania amazonensis amastigotes. Infect. Immun., 2002, 70, 3727-3735.
    • (2002) Infect. Immun. , vol.70 , pp. 3727-3735
    • Holzmuller, P.1    Sereno, D.2    Cavaleyra, M.3    Mangot, I.4    Daulouede, S.5    Vincendeau, P.6    Lemesre, J.L.7
  • 117
    • 0028836685 scopus 로고
    • Mechanisms controlling death, survival and proliferation in a model unicellular eukaryote Tetrahymena thermophila
    • Christensen, S. T.; Wheatley, D. N.; Rasmussen, M. I.; Rasmussen, L. Mechanisms controlling death, survival and proliferation in a model unicellular eukaryote Tetrahymena thermophila. Cell Death Differ., 1995, 2, 301-308.
    • (1995) Cell. Death Differ. , vol.2 , pp. 301-308
    • Christensen, S.T.1    Wheatley, D.N.2    Rasmussen, M.I.3    Rasmussen, L.4
  • 118
    • 0038651013 scopus 로고    scopus 로고
    • Caspase-like activity in programmed nuclear death during conjugation of Tetrahymena thermophila
    • Kobayashi, T.; Endoh, H. Caspase-like activity in programmed nuclear death during conjugation of Tetrahymena thermophila. Cell Death Differ., 2003, 10, 634-640.
    • (2003) Cell. Death Differ. , vol.10 , pp. 634-640
    • Kobayashi, T.1    Endoh, H.2
  • 119
    • 0034954214 scopus 로고    scopus 로고
    • Blastocystis hominis: Evidence for caspase-3-like activity in cells undergoing programmed cell death
    • Nasirudeen, A. M.; Singh, M.; Yap, E. H.; Tan, K. S. Blastocystis hominis: evidence for caspase-3-like activity in cells undergoing programmed cell death. Parasitol. Res., 2001, 87, 559-565.
    • (2001) Parasitol. Res. , vol.87 , pp. 559-565
    • Nasirudeen, A.M.1    Singh, M.2    Yap, E.H.3    Tan, K.S.4
  • 120
    • 0034822447 scopus 로고    scopus 로고
    • Programmed cell death in a human intestinal parasite, Blastocystis hominis
    • DOI 10.1017/S0031182001008332
    • Nasirudeen, A. M.; Tan, K. S.; Singh, M.; Yap, E. H. Programmed cell death in a human intestinal parasite, Blastocystis hominis. Parasitology, 2001, 123, 235-246. (Pubitemid 32881848)
    • (2001) Parasitology , vol.123 , Issue.3 , pp. 235-246
    • Nasirudeen, A.M.A.1    Tan, K.S.W.2    Singh, M.3    Yap, E.H.4
  • 122
    • 0036020254 scopus 로고    scopus 로고
    • Apoptosis in the malaria protozoan, Plasmodium berghei: A possible mechanism for limiting intensity of infection in the mosquito
    • Al-Olayan, E. M.; Williams, G. T.; Hurd, H. Apoptosis in the malaria protozoan, Plasmodium berghei: a possible mechanism for limiting intensity of infection in the mosquito. Int. J. Parasitol., 2002, 32, 1133-1143.
    • (2002) Int. J. Parasitol. , vol.32 , pp. 1133-1143
    • Al-Olayan, E.M.1    Williams, G.T.2    Hurd, H.3
  • 123
    • 34249866547 scopus 로고    scopus 로고
    • Features of apoptosis in Plasmodium falciparum erythrocytic stage through a putative role of PfMCA1 metacaspase-like protein
    • Meslin, B.; Barnadas, C.; Boni, V.; Latour, C.; De Monbrison, F.; Kaiser, K.; Picot, S. Features of apoptosis in Plasmodium falciparum erythrocytic stage through a putative role of PfMCA1 metacaspase-like protein. J. Infect. Dis., 2007, 195, 1852-1859.
    • (2007) J. Infect. Dis. , vol.195 , pp. 1852-1859
    • Meslin, B.1    Barnadas, C.2    Boni, V.3    Latour, C.4    De Monbrison, F.5    Kaiser, K.6    Picot, S.7
  • 124
    • 0033819140 scopus 로고    scopus 로고
    • Programmed death in bacteria
    • Lewis, K. Programmed death in bacteria. Microbiol. Mol. Biol. Rev., 2000, 64, 503-514.
    • (2000) Microbiol. Mol. Biol. Rev. , vol.64 , pp. 503-514
    • Lewis, K.1
  • 125
    • 0035108209 scopus 로고    scopus 로고
    • Programmed cell death in Escherichia coli: Some antibiotics can trigger mazEF lethality
    • Sat, B.; Hazan, R.; Fisher, T.; Khaner, H.; Glaser, G.; Engelberg-Kulka, H. Programmed cell death in Escherichia coli: some antibiotics can trigger mazEF lethality. J. Bacteriol., 2001, 183, 2041-2045.
    • (2001) J. Bacteriol. , vol.183 , pp. 2041-2045
    • Sat, B.1    Hazan, R.2    Fisher, T.3    Khaner, H.4    Glaser, G.5    Engelberg-Kulka, H.6
  • 128
    • 0033598203 scopus 로고    scopus 로고
    • Programmed cell death of the dinoflagellate Peridinium gatunense is mediated by CO[2]limitation and oxidative stress
    • Vardi, A.; Berman-Frank, I.; Rozenberg, T.; Hadas, O.; Kaplan, A.; Levine, A. Programmed cell death of the dinoflagellate Peridinium gatunense is mediated by CO[2]limitation and oxidative stress. Curr. Biol., 1999, 9, 1061-1064.
    • (1999) Curr. Biol. , vol.9 , pp. 1061-1064
    • Vardi, A.1    Berman-Frank, I.2    Rozenberg, T.3    Hadas, O.4    Kaplan, A.5    Levine, A.6
  • 129
    • 0029569160 scopus 로고
    • Evidence for UV-B-induced DNA degradation in Euglena gracilis mediated by activation of metal-dependent nucleases
    • Scheuerlein, R.; Treml, S.; Thar, B.; Tirlapur, U. K.; Hader, D. P. Evidence for UV-B-induced DNA degradation in Euglena gracilis mediated by activation of metal-dependent nucleases. J. Photochem. Photobiol. B., 1995, 31, 113-123.
    • (1995) J. Photochem. Photobiol. B. , vol.31 , pp. 113-123
    • Scheuerlein, R.1    Treml, S.2    Thar, B.3    Tirlapur, U.K.4    Hader, D.P.5
  • 130
    • 0038482128 scopus 로고    scopus 로고
    • The intestinal protozoan parasite Entamoeba histolytica contains 20 cysteine protease genes, of which only a small subset is expressed during in vitro cultivation
    • Bruchhaus, I.; Loftus, B. J.; Hall, N.; Tannich, E. The intestinal protozoan parasite Entamoeba histolytica contains 20 cysteine protease genes, of which only a small subset is expressed during in vitro cultivation. Eukaryot. Cell, 2003, 2, 501-509.
    • (2003) Eukaryot. Cell. , vol.2 , pp. 501-509
    • Bruchhaus, I.1    Loftus, B.J.2    Hall, N.3    Tannich, E.4
  • 133
    • 10644290724 scopus 로고    scopus 로고
    • Camptothecin-induced imbalance in intracellular cation homeostasis regulates programmed cell death in unicellular hemoflagellate Leishmania donovani
    • DOI 10.1074/jbc.M406705200
    • Sen, N.; Das, B. B.; Ganguly, A.; Mukherjee, T.; Bandyopadhyay, S.; Majumder, H. K. Camptothecin-induced imbalance in intracellular cation homeostasis regulates programmed cell death in unicellular hemoflagellate Leishmania donovani. J. Biol. Chem., 2004, 279, 52366-52375. (Pubitemid 39656613)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.50 , pp. 52366-52375
    • Sen, N.1    Das, B.B.2    Ganguly, A.3    Mukherjee, T.4    Bandyopadhyay, S.5    Majumder, H.K.6
  • 134
    • 4344576960 scopus 로고    scopus 로고
    • Camptothecin induced mitochondrial dysfunction leading to programmed cell death in unicellular hemoflagellate Leishmania donovani
    • DOI 10.1038/sj.cdd.4401435
    • Sen, N.; Das, B. B.; Ganguly, A.; Mukherjee, T.; Tripathi, G.; Bandyopadhyay, S.; Rakshit, S.; Sen, T.; Majumder, H. K. Camptothecin induced mitochondrial dysfunction leading to programmed cell death in unicellular hemoflagellate Leishmania donovani. Cell Death Differ., 2004, 11, 924-936. (Pubitemid 39139751)
    • (2004) Cell Death and Differentiation , vol.11 , Issue.8 , pp. 924-936
    • Sen, N.1    Das, B.B.2    Ganguly, A.3    Mukherjee, T.4    Tripathi, G.5    Bandyopadhyay, S.6    Rakshit, S.7    Sen, T.8    Majumder, H.K.9
  • 137
    • 0037165647 scopus 로고    scopus 로고
    • A metacaspase of Trypanosoma brucei causes loss of respiration competence and clonal death in the yeast Saccharomyces cerevisiae
    • Szallies, A.; Kubata, B. K.; Duszenko, M. A metacaspase of Trypanosoma brucei causes loss of respiration competence and clonal death in the yeast Saccharomyces cerevisiae. FEBS Lett., 2002, 517, 144-150.
    • (2002) FEBS Lett. , vol.517 , pp. 144-150
    • Szallies, A.1    Kubata, B.K.2    Duszenko, M.3
  • 138
    • 0142241246 scopus 로고    scopus 로고
    • Pharmacological modulation of Poly (ADP-ribose) polymerase-mediated cell death: Exploitation in cancer chemotherapy
    • Nguewa, P. A.; Fuertes, M. A.; Alonso, C.; Perez, J. M. Pharmacological modulation of Poly (ADP-ribose) polymerase-mediated cell death: exploitation in cancer chemotherapy. Mol. Pharmacol., 2003, 64, 1007-1014.
    • (2003) Mol. Pharmacol. , vol.64 , pp. 1007-1014
    • Nguewa, P.A.1    Fuertes, M.A.2    Alonso, C.3    Perez, J.M.4
  • 140
    • 1942440907 scopus 로고    scopus 로고
    • Plasmodium falciparum-do killers commit suicide?
    • Deponte, M.; Becker, K. Plasmodium falciparum-do killers commit suicide? Trends Parasitol., 2004, 20, 165-169.
    • (2004) Trends Parasitol. , vol.20 , pp. 165-169
    • Deponte, M.1    Becker, K.2
  • 141
    • 0033776271 scopus 로고    scopus 로고
    • Changes in intramitochondrial and cytosolic pH: Early events that modulate caspase activation during apoptosis
    • Matsuyama, S.; Llopis, J.; Deveraux, Q. L.; Tsien, R. Y.; Reed, J. C. Changes in intramitochondrial and cytosolic pH: early events that modulate caspase activation during apoptosis. Nat. Cell Biol., 2000, 2, 318-325.
    • (2000) Nat. Cell. Biol. , vol.2 , pp. 318-325
    • Matsuyama, S.1    Llopis, J.2    Deveraux, Q.L.3    Tsien, R.Y.4    Reed, J.C.5
  • 142
    • 0034523187 scopus 로고    scopus 로고
    • Mitochondria-dependent apoptosis and cellular pH regulation
    • Matsuyama, S.; Reed, J. C. Mitochondria-dependent apoptosis and cellular pH regulation. Cell Death Differ, 2000, 7, 1155-1165.
    • (2000) Cell. Death Differ , vol.7 , pp. 1155-1165
    • Matsuyama, S.1    Reed, J.C.2
  • 143
  • 144
    • 0019941967 scopus 로고
    • Induction of crisis forms in cultured Plasmodium falciparum with human immune serum from Sudan
    • Jensen, J. B.; Boland, M. T.; Akood, M. Induction of crisis forms in cultured Plasmodium falciparum with human immune serum from Sudan. Science, 1982, 216, 1230-1233.
    • (1982) Science , vol.216 , pp. 1230-1233
    • Jensen, J.B.1    Boland, M.T.2    Akood, M.3
  • 145
    • 0022410803 scopus 로고
    • Comparison of inducers of crisis forms in Plasmodium falciparum in vitro
    • Carlin, J. M.; Jensen, J. B.; Geary, T. G. Comparison of inducers of crisis forms in Plasmodium falciparum in vitro. Am. J. Trop. Med. Hyg., 1985, 34, 668-674.
    • (1985) Am. J. Trop. Med. Hyg. , vol.34 , pp. 668-674
    • Carlin, J.M.1    Jensen, J.B.2    Geary, T.G.3
  • 146
    • 0033406341 scopus 로고    scopus 로고
    • CpG DNA rescues B cells from apoptosis by activating NFkappaB and preventing mitochondrial membrane potential disruption via a chloroquine-sensitive pathway
    • Yi, A. K.; Peckham, D. W.; Ashman, R. F.; Krieg, A. M. CpG DNA rescues B cells from apoptosis by activating NFkappaB and preventing mitochondrial membrane potential disruption via a chloroquine-sensitive pathway. Int. Immunol., 1999, 11, 2015-2024.
    • (1999) Int. Immunol. , vol.11 , pp. 2015-2024
    • Yi, A.K.1    Peckham, D.W.2    Ashman, R.F.3    Krieg, A.M.4
  • 147
    • 0035126893 scopus 로고    scopus 로고
    • Early induction of apoptosis in B-chronic lymphocytic leukaemia cells by hydroxychloroquine: Activation of caspase-3 and no protection by survival factors
    • Lagneaux, L.; Delforge, A.; Carlier, S.; Massy, M.; Bernier, M.; Bron, D. Early induction of apoptosis in B-chronic lymphocytic leukaemia cells by hydroxychloroquine: activation of caspase-3 and no protection by survival factors. Br. J. Haematol., 2001, 112, 344-352.
    • (2001) Br. J. Haematol. , vol.112 , pp. 344-352
    • Lagneaux, L.1    Delforge, A.2    Carlier, S.3    Massy, M.4    Bernier, M.5    Bron, D.6
  • 148
    • 3242795805 scopus 로고    scopus 로고
    • Apoptotic cell death kinetics in vitro depend on the cell types and the inducers used
    • Wolbers, F.; Buijtenhuijs, P.; Haanen, C.; Vermes, H. Apoptotic cell death kinetics in vitro depend on the cell types and the inducers used. Apoptosis, 2004, 9, 385-392.
    • (2004) Apoptosis , vol.9 , pp. 385-392
    • Wolbers, F.1    Buijtenhuijs, P.2    Haanen, C.3    Vermes, H.4
  • 149
    • 0242669367 scopus 로고    scopus 로고
    • Data-mining approaches reveal hidden families of proteases in the genome of malaria parasite
    • Wu, Y.; Wang, X.; Liu, X.; Wang, Y. Data-mining approaches reveal hidden families of proteases in the genome of malaria parasite. Genome Res., 2003, 13, 601-616.
    • (2003) Genome Res. , vol.13 , pp. 601-616
    • Wu, Y.1    Wang, X.2    Liu, X.3    Wang, Y.4
  • 150
    • 0024400016 scopus 로고
    • Selective activity of 5-fluoroorotic acid against Plasmodium falciparum in vitro
    • Rathod, P. K.; Khatri, A.; Hubbert, T.; Milhous, W. K. Selective activity of 5-fluoroorotic acid against Plasmodium falciparum in vitro. Antimicrob. Agents Chemother., 1989, 33, 1090-1094.
    • (1989) Antimicrob. Agents Chemother. , vol.33 , pp. 1090-1094
    • Rathod, P.K.1    Khatri, A.2    Hubbert, T.3    Milhous, W.K.4
  • 151
    • 0026510588 scopus 로고
    • Molecular targets of 5-fluoroorotate in the human malaria parasite, Plasmodium falciparum
    • Rathod, P. K.; Leffers, N. P.; Young, R. D. Molecular targets of 5-fluoroorotate in the human malaria parasite, Plasmodium falciparum. Antimicrob. Agents Chemother., 1992, 36, 704-711.
    • (1992) Antimicrob. Agents Chemother. , vol.36 , pp. 704-711
    • Rathod, P.K.1    Leffers, N.P.2    Young, R.D.3
  • 152
    • 60849136008 scopus 로고    scopus 로고
    • Plasmodium berghei: Efficacy of 5-fluoroorotate in combination with commonly used antimalarial drugs in a mouse model
    • Muregi, F. W.; Kano, S.; Kino, H.; Ishih, A. Plasmodium berghei: efficacy of 5-fluoroorotate in combination with commonly used antimalarial drugs in a mouse model. Exp. Parasitol., 2009, 121, 376-380.
    • (2009) Exp. Parasitol. , vol.121 , pp. 376-380
    • Muregi, F.W.1    Kano, S.2    Kino, H.3    Ishih, A.4
  • 153
    • 33750341991 scopus 로고    scopus 로고
    • Apoptosis-like death as a feature of malaria infection in mosquitoes
    • Hurd, H.; Grant, K. M.; Arambage, S. C. Apoptosis-like death as a feature of malaria infection in mosquitoes. Parasitology, 2006, 132 Suppl, S33-47.
    • (2006) Parasitology , vol.132 , Issue.SUPPL.
    • Hurd, H.1    Grant, K.M.2    Arambage, S.C.3
  • 154
    • 0021675954 scopus 로고
    • The biology of Plasmodium in the mosquito
    • Sinden, R. E. The biology of Plasmodium in the mosquito. Experientia, 1984, 40, 1330-1343.
    • (1984) Experientia , vol.40 , pp. 1330-1343
    • Sinden, R.E.1
  • 155
    • 0036854596 scopus 로고    scopus 로고
    • Molecular interactions between Plasmodium and its insect vectors
    • Sinden, R. E. Molecular interactions between Plasmodium and its insect vectors. Cell Microbiol., 2002, 4, 713-724.
    • (2002) Cell. Microbiol. , vol.4 , pp. 713-724
    • Sinden, R.E.1
  • 156
  • 157
    • 0026085210 scopus 로고
    • Plasmodium berghei ookinete densities in three anopheline species
    • Vaughan, J. A.; Narum, D.; Azad, A. F. Plasmodium berghei ookinete densities in three anopheline species. J. Parasitol., 1991, 77, 758-761.
    • (1991) J. Parasitol. , vol.77 , pp. 758-761
    • Vaughan, J.A.1    Narum, D.2    Azad, A.F.3
  • 158
    • 0031952525 scopus 로고    scopus 로고
    • Malaria parasite development in mosquitoes
    • Beier, J. C. Malaria parasite development in mosquitoes. Annu. Rev. Entomol., 1998, 43, 519-543.
    • (1998) Annu. Rev. Entomol. , vol.43 , pp. 519-543
    • Beier, J.C.1
  • 159
    • 0034192006 scopus 로고    scopus 로고
    • The journey of the malaria parasite in the mosquito: Hopes for the new century
    • Ghosh, A.; Edwards, M. J.; Jacobs-Lorena, M. The journey of the malaria parasite in the mosquito: hopes for the new century. Parasitol. Today, 2000, 16, 196-201.
    • (2000) Parasitol. Today , vol.16 , pp. 196-201
    • Ghosh, A.1    Edwards, M.J.2    Jacobs-Lorena, M.3
  • 160
    • 0030764554 scopus 로고    scopus 로고
    • Determinants of malaria-mosquito specificity
    • Billingsley, P. F.; Sinden, R. E. Determinants of malaria-mosquito specificity. Parasitol. Today, 1997, 13, 297-301.
    • (1997) Parasitol. Today , vol.13 , pp. 297-301
    • Billingsley, P.F.1    Sinden, R.E.2
  • 161
    • 0035011519 scopus 로고    scopus 로고
    • Plasmodium invasion of mosquito cells: Hawk or dove?
    • Sinden, R. E.; Billingsley, P. F. Plasmodium invasion of mosquito cells: hawk or dove? Trends Parasitol., 2001, 17, 209-212.
    • (2001) Trends Parasitol. , vol.17 , pp. 209-212
    • Sinden, R.E.1    Billingsley, P.F.2
  • 162
    • 0035895540 scopus 로고    scopus 로고
    • Apoptotic molecular machinery: Vastly increased complexity in vertebrates revealed by genome comparisons
    • Aravind, L.; Dixit, V. M.; Koonin, E. V. Apoptotic molecular machinery: vastly increased complexity in vertebrates revealed by genome comparisons. Science, 2001, 291, 1279-1284.
    • (2001) Science , vol.291 , pp. 1279-1284
    • Aravind, L.1    Dixit, V.M.2    Koonin, E.V.3
  • 163
    • 12744262976 scopus 로고    scopus 로고
    • Cysteine proteases of malaria parasites
    • Rosenthal, P. J. Cysteine proteases of malaria parasites. Int. J. Parasitol., 2004, 34, 1489-1499.
    • (2004) Int. J. Parasitol. , vol.34 , pp. 1489-1499
    • Rosenthal, P.J.1
  • 164
    • 34047158115 scopus 로고    scopus 로고
    • The role of metacaspase 1 in Plasmodium berghei development and apoptosis
    • Le Chat, L.; Sinden, R. E.; Dessens, J. T. The role of metacaspase 1 in Plasmodium berghei development and apoptosis. Mol. Biochem. Parasitol., 2007, 153, 41-47.
    • (2007) Mol. Biochem. Parasitol. , vol.153 , pp. 41-47
    • Le Chat, L.1    Sinden, R.E.2    Dessens, J.T.3
  • 167
    • 0031569532 scopus 로고    scopus 로고
    • Calpain, an upstream regulator of thymocyte apoptosis
    • Squier, M. K.; Cohen, J. J. Calpain, an upstream regulator of thymocyte apoptosis. J. Immunol., 1997, 158, 3690-3697.
    • (1997) J. Immunol. , vol.158 , pp. 3690-3697
    • Squier, M.K.1    Cohen, J.J.2
  • 168
    • 0035971091 scopus 로고    scopus 로고
    • Synergistic activation of caspase-3 by m-calpain after neonatal hypoxia-ischemia: A mechanism of "pathological apoptosis"?
    • Blomgren, K.; Zhu, C.; Wang, X.; Karlsson, J. O.; Leverin, A. L.; Bahr, B. A.; Mallard, C.; Hagberg, H. Synergistic activation of caspase-3 by m-calpain after neonatal hypoxia-ischemia: a mechanism of "pathological apoptosis"? J. Biol. Chem., 2001, 276, 10191-10198.
    • (2001) J. Biol. Chem. , vol.276 , pp. 10191-10198
    • Blomgren, K.1    Zhu, C.2    Wang, X.3    Karlsson, J.O.4    Leverin, A.L.5    Bahr, B.A.6    Mallard, C.7    Hagberg, H.8
  • 170
    • 0036374209 scopus 로고    scopus 로고
    • Lysosomal cathepsins: Structure, role in antigen processing and presentation, and cancer
    • Turk, V.; Turk, B.; Guncar, G.; Turk, D.; Kos, J. Lysosomal cathepsins: structure, role in antigen processing and presentation, and cancer. Adv. Enzyme. Regul, 2002, 42, 285-303.
    • (2002) Adv. Enzyme. Regul , vol.42 , pp. 285-303
    • Turk, V.1    Turk, B.2    Guncar, G.3    Turk, D.4    Kos, J.5
  • 172
    • 0034948738 scopus 로고    scopus 로고
    • The autophagosomal-lysosomal compartment in programmed cell death
    • Bursch, W. The autophagosomal-lysosomal compartment in programmed cell death. Cell Death Differ., 2001, 8, 569-581.
    • (2001) Cell. Death Differ. , vol.8 , pp. 569-581
    • Bursch, W.1
  • 173
    • 0036311492 scopus 로고    scopus 로고
    • On the origin, evolution, and nature of programmed cell death: A timeline of four billion years
    • Ameisen, J. C. On the origin, evolution, and nature of programmed cell death: a timeline of four billion years. Cell Death Differ., 2002, 9, 367-393.
    • (2002) Cell. Death Differ. , vol.9 , pp. 367-393
    • Ameisen, J.C.1
  • 175
    • 0036449793 scopus 로고    scopus 로고
    • Current status of the molecular mechanisms of anticancer druginduced apoptosis. The contribution of molecular-level analysis to cancer chemotherapy
    • Kim, R.; Tanabe, K.; Uchida, Y.; Emi, M.; Inoue, H.; Toge, T. Current status of the molecular mechanisms of anticancer druginduced apoptosis. The contribution of molecular-level analysis to cancer chemotherapy. Cancer Chemother. Pharmacol., 2002, 50, 343-352.
    • (2002) Cancer Chemother. Pharmacol. , vol.50 , pp. 343-352
    • Kim, R.1    Tanabe, K.2    Uchida, Y.3    Emi, M.4    Inoue, H.5    Toge, T.6
  • 176
    • 0037351752 scopus 로고    scopus 로고
    • Programmed cell death in trypanosomatids and other unicellular organisms
    • Debrabant, A.; Lee, N.; Bertholet, S.; Duncan, R.; Nakhasi, H. L. Programmed cell death in trypanosomatids and other unicellular organisms. Int. J. Parasitol., 2003, 33, 257-267.
    • (2003) Int. J. Parasitol. , vol.33 , pp. 257-267
    • Debrabant, A.1    Lee, N.2    Bertholet, S.3    Duncan, R.4    Nakhasi, H.L.5
  • 177
    • 0032898838 scopus 로고    scopus 로고
    • Nitric oxide and cell death
    • Murphy, M. P. Nitric oxide and cell death. Biochim. Biophys. Acta, 1999, 1411, 401-414.
    • (1999) Biochim. Biophys. Acta , vol.1411 , pp. 401-414
    • Murphy, M.P.1
  • 178
    • 78751550717 scopus 로고    scopus 로고
    • Sodium uptake is required for apoptotic cell shrinkage during anti-Fas induced apoptosis
    • Bortner, C.; Cidlowski, J. A. Sodium uptake is required for apoptotic cell shrinkage during anti-Fas induced apoptosis. Cytometry, 2002, 78-78.
    • (2002) Cytometry , pp. 78-78
    • Bortner, C.1    Cidlowski, J.A.2
  • 179
    • 0031451872 scopus 로고    scopus 로고
    • A primary role for K+ and Na+ efflux in the activation of apoptosis
    • Bortner, C. D.; Hughes, F. M., Jr.; Cidlowski, J. A. A primary role for K+ and Na+ efflux in the activation of apoptosis. J. Biol. Chem., 1997, 272, 32436-32442.
    • (1997) J. Biol. Chem. , vol.272 , pp. 32436-32442
    • Bortner, C.D.1    Hughes Jr., F.M.2    Cidlowski, J.A.3
  • 180
    • 0026014249 scopus 로고
    • Artemisinin[qinghaosu]: The role of intracellular hemin in its mechanism of antimalarial action
    • Meshnick, S. R.; Thomas, A.; Ranz, A.; Xu, C. M.; Pan, H. Z. Artemisinin[qinghaosu]: the role of intracellular hemin in its mechanism of antimalarial action. Mol. Biochem. Parasitol., 1991, 49, 181-189.
    • (1991) Mol. Biochem. Parasitol. , vol.49 , pp. 181-189
    • Meshnick, S.R.1    Thomas, A.2    Ranz, A.3    Xu, C.M.4    Pan, H.Z.5
  • 182
    • 0022181111 scopus 로고
    • The chemotherapy of rodent malaria, XXXIX. Ultrastructural changes following treatment with artemisinine of Plasmodium berghei infection in mice, with observations of the localization of (3H)-dihydroartemisinine in P. falciparum in vitro
    • Ellis, D. S.; Li, Z. L.; Gu, H. M.; Peters, W.; Robinson, B. L.; Tovey, G.; Warhurst, D. C. The chemotherapy of rodent malaria, XXXIX. Ultrastructural changes following treatment with artemisinine of Plasmodium berghei infection in mice, with observations of the localization of (3H)-dihydroartemisinine in P. falciparum in vitro. Ann. Trop. Med. Parasitol., 1985, 79, 367-374.
    • (1985) Ann. Trop. Med. Parasitol. , vol.79 , pp. 367-374
    • Ellis, D.S.1    Li, Z.L.2    Gu, H.M.3    Peters, W.4    Robinson, B.L.5    Tovey, G.6    Warhurst, D.C.7
  • 183
    • 0027771695 scopus 로고
    • Morphologic effects of artemether on Plasmodium falciparum in Aotus trivirgatus
    • Kawai, S.; Kano, S.; Suzuki, M. Morphologic effects of artemether on Plasmodium falciparum in Aotus trivirgatus. Am. J. Trop. Med. Hyg., 1993, 49, 812-818.
    • (1993) Am. J. Trop. Med. Hyg. , vol.49 , pp. 812-818
    • Kawai, S.1    Kano, S.2    Suzuki, M.3
  • 184
    • 0021866921 scopus 로고
    • Qinghaosuinduced changes in the morphology of Plasmodium inui
    • Jiang, J. B.; Jacobs, G.; Liang, D. S.; Aikawa, M. Qinghaosuinduced changes in the morphology of Plasmodium inui. Am. J. Trop. Med. Hyg., 1985, 34, 424-428.
    • (1985) Am. J. Trop. Med. Hyg. , vol.34 , pp. 424-428
    • Jiang, J.B.1    Jacobs, G.2    Liang, D.S.3    Aikawa, M.4
  • 186
    • 77949661216 scopus 로고    scopus 로고
    • Artemisinin directly targets malarial mitochondria through its specific mitochondrial activation
    • Wang, J.; Huang, L.; Li, J.; Fan, Q.; Long, Y.; Li, Y.; Zhou, B. Artemisinin directly targets malarial mitochondria through its specific mitochondrial activation. PLoS One, 2010, 5, e9582.
    • (2010) PLoS One , vol.5
    • Wang, J.1    Huang, L.2    Li, J.3    Fan, Q.4    Long, Y.5    Li, Y.6    Zhou, B.7
  • 187
    • 45549109486 scopus 로고    scopus 로고
    • Dihydroartemisinin induces apoptosis in human leukemia cells HL60 via downregulation of transferrin receptor expression
    • Zhou, H. J.; Wang, Z.; Li, A. Dihydroartemisinin induces apoptosis in human leukemia cells HL60 via downregulation of transferrin receptor expression. Anticancer Drugs, 2008, 19, 247-255.
    • (2008) Anticancer Drugs , vol.19 , pp. 247-255
    • Zhou, H.J.1    Wang, Z.2    Li, A.3
  • 188
    • 0022383509 scopus 로고
    • Transferrin receptor: Its biological significance
    • May, W. S. Jr.; Cuatrecasas, P. Transferrin receptor: its biological significance. J. Membr. Biol., 1985, 88, 205-215.
    • (1985) J. Membr. Biol. , vol.88 , pp. 205-215
    • May Jr., W.S.1    Cuatrecasas, P.2
  • 190
    • 0028069902 scopus 로고
    • Iron deprivation-induced apoptosis in HL-60 cells
    • Fukuchi, K.; Tomoyasu, S.; Tsuruoka, N.; Gomi, K. Iron deprivation-induced apoptosis in HL-60 cells. FEBS Lett., 1994, 350, 139-142.
    • (1994) FEBS Lett. , vol.350 , pp. 139-142
    • Fukuchi, K.1    Tomoyasu, S.2    Tsuruoka, N.3    Gomi, K.4
  • 191
    • 0141836226 scopus 로고    scopus 로고
    • Iron deprivation induces apoptosis independently of p53 in human and murine tumour cells
    • Truksa, J.; Kovar, J.; Valenta, T.; Ehrlichova, M.; Polak, J.; Naumann, P. W. Iron deprivation induces apoptosis independently of p53 in human and murine tumour cells. Cell Prolif., 2003, 36, 199-213.
    • (2003) Cell. Prolif. , vol.36 , pp. 199-213
    • Truksa, J.1    Kovar, J.2    Valenta, T.3    Ehrlichova, M.4    Polak, J.5    Naumann, P.W.6
  • 192
    • 0028828562 scopus 로고
    • Heme degradation in the presence of glutathione. A proposed mechanism to account for the high levels of non-heme iron found in the membranes of hemoglobinopathic red blood cells
    • Atamna, H.; Ginsburg, H. Heme degradation in the presence of glutathione. A proposed mechanism to account for the high levels of non-heme iron found in the membranes of hemoglobinopathic red blood cells. J. Biol. Chem., 1995, 270, 24876-24883.
    • (1995) J. Biol. Chem. , vol.270 , pp. 24876-24883
    • Atamna, H.1    Ginsburg, H.2
  • 193
    • 0035060361 scopus 로고    scopus 로고
    • Mode of action and mechanisms of resistance for antimalarial drugs
    • Olliaro, P. Mode of action and mechanisms of resistance for antimalarial drugs. Pharmacol. Ther., 2001, 89, 207-219.
    • (2001) Pharmacol. Ther. , vol.89 , pp. 207-219
    • Olliaro, P.1
  • 194
    • 0030879653 scopus 로고    scopus 로고
    • Hemoglobin metabolism in the malaria parasite Plasmodium falciparum
    • Francis, S. E.; Sullivan, D. J. Jr.; Goldberg, D. E. Hemoglobin metabolism in the malaria parasite Plasmodium falciparum. Annu. Rev. Microbiol., 1997, 51, 97-123.
    • (1997) Annu. Rev. Microbiol. , vol.51 , pp. 97-123
    • Francis, S.E.1    Sullivan Jr., D.J.2    Goldberg, D.E.3
  • 195
    • 0033525824 scopus 로고    scopus 로고
    • The fate of ferriprotorphyrin IX in malaria infected erythrocytes in conjunction with the mode of action of antimalarial drugs
    • Zhang, J.; Krugliak, M.; Ginsburg, H. The fate of ferriprotorphyrin IX in malaria infected erythrocytes in conjunction with the mode of action of antimalarial drugs. Mol. Biochem. Parasitol., 1999, 99, 129-141.
    • (1999) Mol. Biochem. Parasitol. , vol.99 , pp. 129-141
    • Zhang, J.1    Krugliak, M.2    Ginsburg, H.3
  • 196
    • 0025090734 scopus 로고
    • Potentiation of chloroquine activity against Plasmodium falciparum by the peroxidase-hydrogen peroxide system
    • Malhotra, K.; Salmon, D.; Le Bras, J.; Vilde, J. L. Potentiation of chloroquine activity against Plasmodium falciparum by the peroxidase-hydrogen peroxide system. Antimicrob. Agents Chemother., 1990, 34, 1981-1985.
    • (1990) Antimicrob. Agents Chemother. , vol.34 , pp. 1981-1985
    • Malhotra, K.1    Salmon, D.2    Le Bras, J.3    Vilde, J.L.4
  • 197
    • 0036188538 scopus 로고    scopus 로고
    • Mechanisms of resistance of Plasmodium falciparum to antimalarial drugs
    • Hyde, J. E. Mechanisms of resistance of Plasmodium falciparum to antimalarial drugs. Microbes Infect., 2002, 4, 165-174.
    • (2002) Microbes Infect. , vol.4 , pp. 165-174
    • Hyde, J.E.1
  • 198
    • 0028123205 scopus 로고
    • Mitochondrial protein import: Mechanisms, components and energetics
    • DOI 10.1016/0005-2728(94)90125-2
    • Schwarz, E.; Neupert, W. Mitochondrial protein import: mechanisms, components and energetics. Biochim. Biophys. Acta, 1994, 1187, 270-274. (Pubitemid 24267069)
    • (1994) Biochimica et Biophysica Acta - Bioenergetics , vol.1187 , Issue.2 , pp. 270-274
    • Schwarz, E.1    Neupert, W.2
  • 200
    • 0028903933 scopus 로고
    • Reduction in mitochondrial potential constitutes an early irreversible step of programmed lymphocyte death in vivo
    • Zamzami, N.; Marchetti, P.; Castedo, M.; Zanin, C.; Vayssiere, J. L.; Petit, P. X.; Kroemer, G. Reduction in mitochondrial potential constitutes an early irreversible step of programmed lymphocyte death in vivo. J. Exp. Med., 1995, 181, 1661-1672.
    • (1995) J. Exp. Med. , vol.181 , pp. 1661-1672
    • Zamzami, N.1    Marchetti, P.2    Castedo, M.3    Zanin, C.4    Vayssiere, J.L.5    Petit, P.X.6    Kroemer, G.7
  • 201
    • 0029983059 scopus 로고    scopus 로고
    • Inhibitors of permeability transition interfere with the disruption of the mitochondrial transmembrane potential during apoptosis
    • Zamzami, N.; Marchetti, P.; Castedo, M.; Hirsch, T.; Susin, S. A.; Masse, B.; Kroemer, G. Inhibitors of permeability transition interfere with the disruption of the mitochondrial transmembrane potential during apoptosis. FEBS Lett., 1996, 384, 53-57.
    • (1996) FEBS Lett. , vol.384 , pp. 53-57
    • Zamzami, N.1    Marchetti, P.2    Castedo, M.3    Hirsch, T.4    Susin, S.A.5    Masse, B.6    Kroemer, G.7
  • 203
    • 0027485950 scopus 로고
    • Temporal analysis of events associated with programmed cell death (apoptosis) of sympathetic neurons deprived of nerve growth factor
    • Deckwerth, T. L.; Johnson, E. M. Jr. Temporal analysis of events associated with programmed cell death (apoptosis) of sympathetic neurons deprived of nerve growth factor. J. Cell Biol., 1993, 123, 1207-1222.
    • (1993) J. Cell. Biol. , vol.123 , pp. 1207-1222
    • Deckwerth, T.L.1    Johnson Jr., E.M.2
  • 204
    • 0024930934 scopus 로고
    • The causal prophylactic activity of the novel hydroxynaphthoquinone 566C80 against Plasmodium berghei infections in rats
    • Davies, C. S.; Pudney, M.; Matthews, P. J.; Sinden, R. E. The causal prophylactic activity of the novel hydroxynaphthoquinone 566C80 against Plasmodium berghei infections in rats. Acta Leiden., 1989, 58, 115-128.
    • (1989) Acta Leiden. , vol.58 , pp. 115-128
    • Davies, C.S.1    Pudney, M.2    Matthews, P.J.3    Sinden, R.E.4
  • 205
    • 0027389953 scopus 로고
    • The novel hydroxynaphthoquinone 566C80 inhibits the development of liver stages of Plasmodium berghei cultured in vitro
    • Davies, C. S.; Pudney, M.; Nicholas, J. C.; Sinden, R. E. The novel hydroxynaphthoquinone 566C80 inhibits the development of liver stages of Plasmodium berghei cultured in vitro. Parasitology, 1993, 106, 1-6.
    • (1993) Parasitology , vol.106 , pp. 1-6
    • Davies, C.S.1    Pudney, M.2    Nicholas, J.C.3    Sinden, R.E.4
  • 206
    • 0029016355 scopus 로고
    • Inhibitory activity of the anti-malarial atovaquone (566C80) against ookinetes, oocysts, and sporozoites of Plasmodium berghei
    • Fowler, R. E.; Sinden, R. E.; Pudney, M. Inhibitory activity of the anti-malarial atovaquone (566C80) against ookinetes, oocysts, and sporozoites of Plasmodium berghei. J. Parasitol., 1995, 81, 452-458.
    • (1995) J. Parasitol. , vol.81 , pp. 452-458
    • Fowler, R.E.1    Sinden, R.E.2    Pudney, M.3
  • 207
    • 0035374621 scopus 로고    scopus 로고
    • Calcium is a key signaling molecule in beta-lapachonemediated cell death
    • Tagliarino, C.; Pink, J. J.; Dubyak, G. R.; Nieminen, A. L.; Boothman, D. A. Calcium is a key signaling molecule in beta-lapachonemediated cell death. J. Biol. Chem., 2001, 276, 19150-19159.
    • (2001) J. Biol. Chem. , vol.276 , pp. 19150-19159
    • Tagliarino, C.1    Pink, J.J.2    Dubyak, G.R.3    Nieminen, A.L.4    Boothman, D.A.5
  • 208
    • 0034009970 scopus 로고    scopus 로고
    • NAD (P) H:Quinone oxidoreductase activity is the principal determinant of beta-lapachone cytotoxicity
    • Pink, J. J.; Planchon, S. M.; Tagliarino, C.; Varnes, M. E.; Siegel, D.; Boothman, D. A. NAD (P) H:Quinone oxidoreductase activity is the principal determinant of beta-lapachone cytotoxicity. J. Biol. Chem., 2000, 275, 5416-5424.
    • (2000) J. Biol. Chem. , vol.275 , pp. 5416-5424
    • Pink, J.J.1    Planchon, S.M.2    Tagliarino, C.3    Varnes, M.E.4    Siegel, D.5    Boothman, D.A.6
  • 211
    • 0037366133 scopus 로고    scopus 로고
    • Biochemical modulation of Cisplatin mechanisms of action: Enhancement of antitumor activity and circumvention of drug resistance
    • Fuertes, M. A.; Alonso, C.; Perez, J. M. Biochemical modulation of Cisplatin mechanisms of action: enhancement of antitumor activity and circumvention of drug resistance. Chem. Rev., 2003, 103, 645-662.
    • (2003) Chem. Rev. , vol.103 , pp. 645-662
    • Fuertes, M.A.1    Alonso, C.2    Perez, J.M.3
  • 212
    • 0028865245 scopus 로고
    • Posttranslational modification of poly (ADP-ribose) polymerase induced by DNA strand breaks
    • Lindahl, T.; Satoh, M. S.; Poirier, G. G.; Klungland, A. Posttranslational modification of poly (ADP-ribose) polymerase induced by DNA strand breaks. Trends Biochem. Sci., 1995, 20, 405-411.
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 405-411
    • Lindahl, T.1    Satoh, M.S.2    Poirier, G.G.3    Klungland, A.4
  • 213
    • 0033198919 scopus 로고    scopus 로고
    • Poly (ADP-ribosyl) ation reactions in the regulation of nuclear functions
    • D'Amours, D.; Desnoyers, S.; D'Silva, I.; Poirier, G. G. Poly (ADP-ribosyl) ation reactions in the regulation of nuclear functions. Biochem. J., 1999, 342, 249-268.
    • (1999) Biochem. J. , vol.342 , pp. 249-268
    • D'Amours, D.1    Desnoyers, S.2    D'Silva, I.3    Poirier, G.G.4
  • 216
    • 0034889007 scopus 로고    scopus 로고
    • Rapamycin blocks IL-2-driven T cell cycle progression while preserving T cell survival
    • Gonzalez, J.; Harris, T.; Childs, G.; Prystowsky, M. B. Rapamycin blocks IL-2-driven T cell cycle progression while preserving T cell survival. Blood Cells Mol. Dis., 2001, 27, 572-585.
    • (2001) Blood Cells Mol. Dis. , vol.27 , pp. 572-585
    • Gonzalez, J.1    Harris, T.2    Childs, G.3    Prystowsky, M.B.4
  • 217
    • 0035060354 scopus 로고    scopus 로고
    • Is cisplatin-induced cell death always produced by apoptosis?
    • Gonzalez, V. M.; Fuertes, M. A.; Alonso, C.; Perez, J. M. Is cisplatin-induced cell death always produced by apoptosis? Mol. Pharmacol., 2001, 59, 657-663.
    • (2001) Mol. Pharmacol. , vol.59 , pp. 657-663
    • Gonzalez, V.M.1    Fuertes, M.A.2    Alonso, C.3    Perez, J.M.4
  • 220
    • 0028540951 scopus 로고
    • (Structure of chromatin. I: Levels of DNA organization in the nucleus; nucleosome and chromatin fibres)
    • Santisteban, M. S. (Structure of chromatin. I: Levels of DNA organization in the nucleus; nucleosome and chromatin fibres). Patho. Biol. Paris, 1994, 42, 868-883.
    • (1994) Patho. Biol. Paris , vol.42 , pp. 868-883
    • Santisteban, M.S.1
  • 221
    • 0024329202 scopus 로고
    • Biochemical characteristics and physiological significance of major DNA topoisomerases
    • Sutcliffe, J. A.; Gootz, T. D.; Barrett, J. F. Biochemical characteristics and physiological significance of major DNA topoisomerases. Antimicrob. Agents Chemother., 1989, 33, 2027-2033.
    • (1989) Antimicrob. Agents Chemother. , vol.33 , pp. 2027-2033
    • Sutcliffe, J.A.1    Gootz, T.D.2    Barrett, J.F.3
  • 222
    • 0025800372 scopus 로고
    • DNA topoisomerases: Why so many?
    • Wang, J. C. DNA topoisomerases: why so many? J. Biol. Chem., 1991, 266, 6659-6662.
    • (1991) J. Biol. Chem. , vol.266 , pp. 6659-6662
    • Wang, J.C.1
  • 223
    • 0034923502 scopus 로고    scopus 로고
    • DNA topoisomerases: Structure, function, and mechanism
    • Champoux, J. J. DNA topoisomerases: structure, function, and mechanism. Annu. Rev. Biochem., 2001, 70, 369-413.
    • (2001) Annu. Rev. Biochem. , vol.70 , pp. 369-413
    • Champoux, J.J.1
  • 224
    • 68949108016 scopus 로고    scopus 로고
    • Functional expression of a DNA-topoisomerase IB from Cryptosporidium parvum
    • Ordonez, C.; Alfonso, J.; Balana-Fouce, R.; Ordonez, D. Functional expression of a DNA-topoisomerase IB from Cryptosporidium parvum. J. Biomed. Biotechnol., 2009, 2009, 837608.
    • (2009) J. Biomed. Biotechnol. , vol.2009 , pp. 837608
    • Ordonez, C.1    Alfonso, J.2    Balana-Fouce, R.3    Ordonez, D.4
  • 225
    • 0021333644 scopus 로고
    • Mechanism of antitumor drug action: Poisoning of mammalian DNA topoisomerase II on DNA by 4'-(9-acridinylamino)-methanesulfon-m-anisidide
    • Nelson, E. M.; Tewey, K. M.; Liu, L. F. Mechanism of antitumor drug action: poisoning of mammalian DNA topoisomerase II on DNA by 4'-(9-acridinylamino)-methanesulfon-m-anisidide. Proc. Natl. Acad. Sci. U. S. A., 1984, 81, 1361-1365.
    • (1984) Proc. Natl. Acad. Sci. U. S. A. , vol.81 , pp. 1361-1365
    • Nelson, E.M.1    Tewey, K.M.2    Liu, L.F.3
  • 226
    • 0035254661 scopus 로고    scopus 로고
    • Apoptotic response of HL-60 human leukemia cells to the antitumor drug NB-506, a glycosylated indolocarbazole inhibitor of topoisomerase 1
    • Facompre, M.; Goossens, J. F.; Bailly, C. Apoptotic response of HL-60 human leukemia cells to the antitumor drug NB-506, a glycosylated indolocarbazole inhibitor of topoisomerase 1. Biochem. Pharmacol., 2001, 61, 299-310.
    • (2001) Biochem. Pharmacol. , vol.61 , pp. 299-310
    • Facompre, M.1    Goossens, J.F.2    Bailly, C.3
  • 227
    • 0034234657 scopus 로고    scopus 로고
    • The topoisomerases of protozoan parasites
    • Cheesman, S. J. The topoisomerases of protozoan parasites. Parasitol. Today, 2000, 16, 277-281.
    • (2000) Parasitol. Today , vol.16 , pp. 277-281
    • Cheesman, S.J.1
  • 228
    • 0027422826 scopus 로고
    • In vitro sensitivity of Plasmodium falciparum to drugs that bind DNA or inhibit its synthesis
    • Lee, S.; Inselburg, J. In vitro sensitivity of Plasmodium falciparum to drugs that bind DNA or inhibit its synthesis. J. Parasitol., 1993, 79, 780-782.
    • (1993) J. Parasitol. , vol.79 , pp. 780-782
    • Lee, S.1    Inselburg, J.2
  • 229
    • 0023263288 scopus 로고
    • Analysis of sequences from the extremely A + T-rich genome of Plasmodium falciparum
    • Weber, J. L. Analysis of sequences from the extremely A + T-rich genome of Plasmodium falciparum. Gene, 1987, 52, 103-109.
    • (1987) Gene , vol.52 , pp. 103-109
    • Weber, J.L.1
  • 230
    • 0020349256 scopus 로고
    • Homologous pairing and strand exchange in genetic recombination
    • Radding, C. M. Homologous pairing and strand exchange in genetic recombination. Annu. Rev. Genet., 1982, 16, 405-437.
    • (1982) Annu. Rev. Genet. , vol.16 , pp. 405-437
    • Radding, C.M.1
  • 231
  • 233
    • 0031627508 scopus 로고    scopus 로고
    • Domains of human topoisomerase I and associated functions
    • Champoux, J. J. Domains of human topoisomerase I and associated functions. Prog. Nucleic Acid Res. Mol. Biol., 1998, 60, 111-132.
    • (1998) Prog. Nucleic Acid Res. Mol. Biol. , vol.60 , pp. 111-132
    • Champoux, J.J.1
  • 234
    • 0025893984 scopus 로고
    • Antagonism between camptothecin and topoisomerase II-directed chemotherapeutic agents in a human leukemia cell line
    • Kaufmann, S. H. Antagonism between camptothecin and topoisomerase II-directed chemotherapeutic agents in a human leukemia cell line. Cancer Res., 1991, 51, 1129-1136.
    • (1991) Cancer Res. , vol.51 , pp. 1129-1136
    • Kaufmann, S.H.1
  • 235
    • 0025133118 scopus 로고
    • Involvement of nucleic acid synthesis in cell killing mechanisms of topoisomerase poisons
    • D'Arpa, P.; Beardmore, C.; Liu, L. F. Involvement of nucleic acid synthesis in cell killing mechanisms of topoisomerase poisons. Cancer Res., 1990, 50, 6919-6924.
    • (1990) Cancer Res. , vol.50 , pp. 6919-6924
    • D'Arpa, P.1    Beardmore, C.2    Liu, L.F.3
  • 236
    • 0026594602 scopus 로고
    • Sequential administration of camptothecin and etoposide circumvents the antagonistic cytotoxicity of simultaneous drug administration in slowly growing human colon carcinoma HT-29 cells
    • Bertrand, R.; O'Connor, P. M.; Kerrigan, D.; Pommier, Y. Sequential administration of camptothecin and etoposide circumvents the antagonistic cytotoxicity of simultaneous drug administration in slowly growing human colon carcinoma HT-29 cells. Eur. J. Cancer, 1992, 28 A, 743-748.
    • (1992) Eur. J. Cancer , vol.28 A , pp. 743-748
    • Bertrand, R.1    O'Connor, P.M.2    Kerrigan, D.3    Pommier, Y.4
  • 238
    • 0025696390 scopus 로고
    • Hypersensitivity to clinically useful alkylating agents and radiation in poly (ADP-ribose) polymerase-deficient cell lines
    • Chatterjee, S.; Cheng, M. F.; Berger, N. A. Hypersensitivity to clinically useful alkylating agents and radiation in poly (ADP-ribose) polymerase-deficient cell lines. Cancer Commun., 1990, 2, 401-407.
    • (1990) Cancer Commun. , vol.2 , pp. 401-407
    • Chatterjee, S.1    Cheng, M.F.2    Berger, N.A.3
  • 239
    • 0024836733 scopus 로고
    • Camptothecin hypersensitivity in poly (adenosine diphosphateribose) polymerase-deficient cell lines
    • Chatterjee, S.; Cheng, M. F.; Trivedi, D.; Petzold, S. J.; Berger, N. A. Camptothecin hypersensitivity in poly (adenosine diphosphateribose) polymerase-deficient cell lines. Cancer Commun., 1989, 1, 389-394.
    • (1989) Cancer Commun. , vol.1 , pp. 389-394
    • Chatterjee, S.1    Cheng, M.F.2    Trivedi, D.3    Petzold, S.J.4    Berger, N.A.5
  • 240
    • 0033799839 scopus 로고    scopus 로고
    • Multidrug resistance (MDR) in cancer. Mechanisms, reversal using modulators of MDR and the role of MDR modulators in influencing the pharmacokinetics of anticancer drugs
    • Krishna, R.; Mayer, L. D. Multidrug resistance (MDR) in cancer. Mechanisms, reversal using modulators of MDR and the role of MDR modulators in influencing the pharmacokinetics of anticancer drugs. Eur. J. Pharm. Sci., 2000, 11, 265-283.
    • (2000) Eur. J. Pharm. Sci. , vol.11 , pp. 265-283
    • Krishna, R.1    Mayer, L.D.2
  • 241
    • 0027484629 scopus 로고
    • Dual topoisomerase I and II inhibition by intoplicine (RP-60475), a new antitumor agent in early clinical trials
    • Poddevin, B.; Riou, J. F.; Lavelle, F.; Pommier, Y. Dual topoisomerase I and II inhibition by intoplicine (RP-60475), a new antitumor agent in early clinical trials. Mol. Pharmacol., 1993, 44, 767-774.
    • (1993) Mol. Pharmacol. , vol.44 , pp. 767-774
    • Poddevin, B.1    Riou, J.F.2    Lavelle, F.3    Pommier, Y.4
  • 242
    • 0030699166 scopus 로고    scopus 로고
    • Dual topoisomerase I/II poisons as anticancer drugs
    • Denny, W. A. Dual topoisomerase I/II poisons as anticancer drugs. Expert Opin. Investig. Drugs, 1997, 6, 1845-1851.
    • (1997) Expert Opin. Investig. Drugs , vol.6 , pp. 1845-1851
    • Denny, W.A.1
  • 243
    • 0025866667 scopus 로고
    • Induction of mammalian DNA topoisomerase I and II mediated DNA cleavage by saintopin, a new antitumor agent from fungus
    • Yamashita, Y.; Kawada, S.; Fujii, N.; Nakano, H. Induction of mammalian DNA topoisomerase I and II mediated DNA cleavage by saintopin, a new antitumor agent from fungus. Biochemistry, 1991, 30, 5838-5845.
    • (1991) Biochemistry , vol.30 , pp. 5838-5845
    • Yamashita, Y.1    Kawada, S.2    Fujii, N.3    Nakano, H.4
  • 244
    • 0027137938 scopus 로고
    • Intoplicine (RP 60475) and its derivatives, a new class of antitumor agents inhibiting both topoisomerase I and II activities
    • Riou, J. F.; Fosse, P.; Nguyen, C. H.; Larsen, A. K.; Bissery, M. C.; Grondard, L.; Saucier, J. M.; Bisagni, E.; Lavelle, F. Intoplicine (RP 60475) and its derivatives, a new class of antitumor agents inhibiting both topoisomerase I and II activities. Cancer Res., 1993, 53, 5987-5993.
    • (1993) Cancer Res. , vol.53 , pp. 5987-5993
    • Riou, J.F.1    Fosse, P.2    Nguyen, C.H.3    Larsen, A.K.4    Bissery, M.C.5    Grondard, L.6    Saucier, J.M.7    Bisagni, E.8    Lavelle, F.9
  • 246
    • 0029761654 scopus 로고    scopus 로고
    • Peptidyl anthraquinones as potential antineoplastic drugs: Synthesis, DNA binding, redox cycling, and biological activity
    • Gatto, B.; Zagotto, G.; Sissi, C.; Cera, C.; Uriarte, E.; Palu, G.; Capranico, G.; Palumbo, M. Peptidyl anthraquinones as potential antineoplastic drugs: synthesis, DNA binding, redox cycling, and biological activity. J. Med. Chem., 1996, 39, 3114-3122.
    • (1996) J. Med. Chem. , vol.39 , pp. 3114-3122
    • Gatto, B.1    Zagotto, G.2    Sissi, C.3    Cera, C.4    Uriarte, E.5    Palu, G.6    Capranico, G.7    Palumbo, M.8
  • 247
    • 0029947975 scopus 로고    scopus 로고
    • Identification of topoisomerase I as the cytotoxic target of the protoberberine alkaloid coralyne
    • Gatto, B.; Sanders, M. M.; Yu, C.; Wu, H. Y.; Makhey, D.; La-Voie, E. J.; Liu, L. F. Identification of topoisomerase I as the cytotoxic target of the protoberberine alkaloid coralyne. Cancer Res, 1996, 56, 2795-2800.
    • (1996) Cancer Res. , vol.56 , pp. 2795-2800
    • Gatto, B.1    Sanders, M.M.2    Yu, C.3    Wu, H.Y.4    Makhey, D.5    La-Voie, E.J.6    Liu, L.F.7
  • 248
    • 0029027350 scopus 로고
    • Biochemistry of topoisomerase I and II inhibition by anthracenyl-amino acid conjugates
    • Meikle, I.; Cummings, J.; Macpherson, J. S.; Hadfield, J. A.; Smyth, J. F. Biochemistry of topoisomerase I and II inhibition by anthracenyl-amino acid conjugates. Biochem. Pharmacol., 1995, 49, 1747-1757.
    • (1995) Biochem. Pharmacol. , vol.49 , pp. 1747-1757
    • Meikle, I.1    Cummings, J.2    Macpherson, J.S.3    Hadfield, J.A.4    Smyth, J.F.5
  • 249
    • 0028818643 scopus 로고
    • Identification of anthracenyl-dipeptide conjugates as novel topoisomerase I and II inhibitors and their evaluation as potential anticancer drugs
    • Meikle, I.; Cummings, J.; Macpherson, J. S.; Smyth, J. F. Identification of anthracenyl-dipeptide conjugates as novel topoisomerase I and II inhibitors and their evaluation as potential anticancer drugs. Anticancer Drug Des, 1995, 10, 515-527.
    • (1995) Anticancer Drug Des. , vol.10 , pp. 515-527
    • Meikle, I.1    Cummings, J.2    Macpherson, J.S.3    Smyth, J.F.4
  • 250
    • 0030580063 scopus 로고    scopus 로고
    • Development of anthracenyl-amino acid conjugates as topoisomerase I and II inhibitors that circumvent drug resistance
    • Cummings, J.; Macpherson, J. S.; Meikle, I.; Smyth, J. F. Development of anthracenyl-amino acid conjugates as topoisomerase I and II inhibitors that circumvent drug resistance. Biochem. Pharmacol., 1996, 52, 979-990.
    • (1996) Biochem. Pharmacol. , vol.52 , pp. 979-990
    • Cummings, J.1    Macpherson, J.S.2    Meikle, I.3    Smyth, J.F.4
  • 251
    • 0031040159 scopus 로고    scopus 로고
    • The potential of N-[2-(dimethylamino) ethyl]acridine-4-carboxamide to circumvent three multidrugresistance phenotypes in vitro
    • Davey, R. A.; Su, G. M.; Hargrave, R. M.; Harvie, R. M.; Baguley, B. C.; Davey, M. W. The potential of N-[2-(dimethylamino) ethyl]acridine-4-carboxamide to circumvent three multidrugresistance phenotypes in vitro. Cancer Chemother. Pharmacol., 1997, 39, 424-430.
    • (1997) Cancer Chemother. Pharmacol. , vol.39 , pp. 424-430
    • Davey, R.A.1    Su, G.M.2    Hargrave, R.M.3    Harvie, R.M.4    Baguley, B.C.5    Davey, M.W.6
  • 253
    • 0028283890 scopus 로고
    • Acquired resistance to cisplatin and doxorubicin in a small cell lung cancer cell line is correlated to elevated expression of glutathione-linked detoxification enzymes
    • Hao, X. Y.; Bergh, J.; Brodin, O.; Hellman, U.; Mannervik, B. Acquired resistance to cisplatin and doxorubicin in a small cell lung cancer cell line is correlated to elevated expression of glutathione-linked detoxification enzymes. Carcinogenesis, 1994, 15, 1167-1173.
    • (1994) Carcinogenesis , vol.15 , pp. 1167-1173
    • Hao, X.Y.1    Bergh, J.2    Brodin, O.3    Hellman, U.4    Mannervik, B.5
  • 254
    • 0026210179 scopus 로고
    • Mechanisms of resistance to drugs that inhibit DNA topoisomerases
    • Beck, W. T.; Danks, M. K. Mechanisms of resistance to drugs that inhibit DNA topoisomerases. Semin. Cancer Biol., 1991, 2, 235-244.
    • (1991) Semin. Cancer Biol. , vol.2 , pp. 235-244
    • Beck, W.T.1    Danks, M.K.2
  • 255
    • 18544393471 scopus 로고    scopus 로고
    • Binding of etoposide to topoisomerase II in the absence of DNA: Decreased affinity as a mechanism of drug resistance
    • DOI 10.1021/bi982855i
    • Kingma, P. S.; Burden, D. A.; Osheroff, N. Binding of etoposide to topoisomerase II in the absence of DNA: decreased affinity as a mechanism of drug resistance. Biochemistry, 1999, 38, 3457-3461. (Pubitemid 29149463)
    • (1999) Biochemistry , vol.38 , Issue.12 , pp. 3457-3461
    • Kingma, P.S.1    Burden, D.A.2    Osheroff, N.3
  • 256
    • 33645471331 scopus 로고    scopus 로고
    • MAMSA resistant human topoisomerase IIbeta mutation G465D has reduced AT P hydrolysis activity
    • Gilroy, K. L.; Leontiou, C.; Padget, K.; Lakey, J. H.; Austin, C. A. mAMSA resistant human topoisomerase IIbeta mutation G465D has reduced AT P hydrolysis activity. Nucleic Acids Res., 2006, 34, 1597-1607.
    • (2006) Nucleic Acids Res. , vol.34 , pp. 1597-1607
    • Gilroy, K.L.1    Leontiou, C.2    Padget, K.3    Lakey, J.H.4    Austin, C.A.5
  • 257
    • 0034079789 scopus 로고    scopus 로고
    • Mutations at arg486 and glu571 in human topoisomerase IIalpha confer resistance to amsacrine: Relevance for antitumor drug resistance in human cells
    • Patel, S.; Keller, B. A.; Fisher, L. M. Mutations at arg486 and glu571 in human topoisomerase IIalpha confer resistance to amsacrine: relevance for antitumor drug resistance in human cells. Mol. Pharmacol., 2000, 57, 784-791.
    • (2000) Mol. Pharmacol. , vol.57 , pp. 784-791
    • Patel, S.1    Keller, B.A.2    Fisher, L.M.3
  • 258
    • 0036644899 scopus 로고    scopus 로고
    • Novel mutation of topoisomerase I in rendering cells resistant to camptothecin
    • Chang, J. Y.; Liu, J. F.; Juang, S. H.; Liu, T. W.; Chen, L. T. Novel mutation of topoisomerase I in rendering cells resistant to camptothecin. Cancer Res., 2002, 62, 3716-3721.
    • (2002) Cancer Res. , vol.62 , pp. 3716-3721
    • Chang, J.Y.1    Liu, J.F.2    Juang, S.H.3    Liu, T.W.4    Chen, L.T.5
  • 259
    • 0027368901 scopus 로고
    • Cloning of Chinese hamster DNA topoisomerase I cDNA and identification of a single point mutation responsible for camptothecin resistance
    • Tanizawa, A.; Beitrand, R.; Kohlhagen, G.; Tabuchi, A.; Jenkins, J.; Pommier, Y. Cloning of Chinese hamster DNA topoisomerase I cDNA and identification of a single point mutation responsible for camptothecin resistance. J. Biol. Chem., 1993, 268, 25463-25468.
    • (1993) J. Biol. Chem. , vol.268 , pp. 25463-25468
    • Tanizawa, A.1    Beitrand, R.2    Kohlhagen, G.3    Tabuchi, A.4    Jenkins, J.5    Pommier, Y.6
  • 260
    • 0028070579 scopus 로고
    • Using yeast to study resistance to topoisomerase II-targeting drugs
    • Nitiss, J. L. Using yeast to study resistance to topoisomerase II-targeting drugs. Cancer Chemother. Pharmacol., 1994, 34 Suppl, S6-13.
    • (1994) Cancer Chemother. Pharmacol. , vol.34 , Issue.SUPPL.
    • Nitiss, J.L.1
  • 261
    • 0027943382 scopus 로고
    • Mutations in the gyrB domain of eukaryotic topoisomerase II can lead to partially dominant resistance to etoposide and amsacrine
    • Nitiss, J. L.; Vilalta, P. M.; Wu, H.; McMahon, J. Mutations in the gyrB domain of eukaryotic topoisomerase II can lead to partially dominant resistance to etoposide and amsacrine. Mol. Pharmacol., 1994, 46, 773-777.
    • (1994) Mol. Pharmacol. , vol.46 , pp. 773-777
    • Nitiss, J.L.1    Vilalta, P.M.2    Wu, H.3    McMahon, J.4
  • 263
    • 33748755472 scopus 로고    scopus 로고
    • The past, present and future of antifolates in the treatment of Plasmodium falciparum infection
    • Nzila, A. The past, present and future of antifolates in the treatment of Plasmodium falciparum infection. J. Antimicrob. Chemother., 2006, 57, 1043-1054.
    • (2006) J. Antimicrob. Chemother. , vol.57 , pp. 1043-1054
    • Nzila, A.1
  • 264
    • 0034065697 scopus 로고    scopus 로고
    • Towards an understanding of the mechanism of pyrimethamine-sulfadoxine resistance in Plasmodium falciparum: Genotyping of dihydrofolate reductase and dihydropteroate synthase of Kenyan parasites
    • Nzila, A. M.; Mberu, E. K.; Sulo, J.; Dayo, H.; Winstanley, P. A.; Sibley, C. H.; Watkins, W. M. Towards an understanding of the mechanism of pyrimethamine-sulfadoxine resistance in Plasmodium falciparum: genotyping of dihydrofolate reductase and dihydropteroate synthase of Kenyan parasites. Antimicrob. Agents Chemother., 2000, 44, 991-996.
    • (2000) Antimicrob. Agents Chemother. , vol.44 , pp. 991-996
    • Nzila, A.M.1    Mberu, E.K.2    Sulo, J.3    Dayo, H.4    Winstanley, P.A.5    Sibley, C.H.6    Watkins, W.M.7
  • 265
    • 0033931237 scopus 로고    scopus 로고
    • Mutations in Plasmodium falciparum cytochrome b that are associated with atovaquone resistance are located at a putative drug-binding site
    • Korsinczky, M.; Chen, N.; Kotecka, B.; Saul, A.; Rieckmann, K.; Cheng, Q. Mutations in Plasmodium falciparum cytochrome b that are associated with atovaquone resistance are located at a putative drug-binding site. Antimicrob. Agents Chemother., 2000, 44, 2100-2108.
    • (2000) Antimicrob. Agents Chemother. , vol.44 , pp. 2100-2108
    • Korsinczky, M.1    Chen, N.2    Kotecka, B.3    Saul, A.4    Rieckmann, K.5    Cheng, Q.6
  • 267
    • 0026772298 scopus 로고
    • Effect of P-glycoprotein expression on the accumulation and cytotoxicity of topotecan (SK&F 104864), a new camptothecin analogue
    • Hendricks, C. B.; Rowinsky, E. K.; Grochow, L. B.; Donehower, R. C.; Kaufmann, S. H. Effect of P-glycoprotein expression on the accumulation and cytotoxicity of topotecan (SK&F 104864), a new camptothecin analogue. Cancer Res., 1992, 52, 2268-2278.
    • (1992) Cancer Res. , vol.52 , pp. 2268-2278
    • Hendricks, C.B.1    Rowinsky, E.K.2    Grochow, L.B.3    Donehower, R.C.4    Kaufmann, S.H.5
  • 268
    • 0024338609 scopus 로고
    • Amplification of the multidrug resistance gene in some chloroquineresistant isolates of P
    • Foote, S. J.; Thompson, J. K.; Cowman, A. F.; Kemp, D. J. Amplification of the multidrug resistance gene in some chloroquineresistant isolates of P. falciparum. Cell, 1989, 57, 921-930.
    • (1989) Falciparum. Cell. , vol.57 , pp. 921-930
    • Foote, S.J.1    Thompson, J.K.2    Cowman, A.F.3    Kemp, D.J.4
  • 269
    • 0024356582 scopus 로고
    • Amplification of a gene related to mammalian mdr genes in drug-resistant Plasmodium falciparum
    • Wilson, C. M.; Serrano, A. E.; Wasley, A.; Bogenschutz, M. P.; Shankar, A. H.; Wirth, D. F. Amplification of a gene related to mammalian mdr genes in drug-resistant Plasmodium falciparum. Science, 1989, 244, 1184-1186.
    • (1989) Science , vol.244 , pp. 1184-1186
    • Wilson, C.M.1    Serrano, A.E.2    Wasley, A.3    Bogenschutz, M.P.4    Shankar, A.H.5    Wirth, D.F.6
  • 270
    • 0026028916 scopus 로고
    • The P-glycoprotein homologues of Plasmodium falciparum: Are they involved in chloroquine resistance?
    • Cowman, A. F. The P-glycoprotein homologues of Plasmodium falciparum: Are they involved in chloroquine resistance? Parasitol. Today, 1991, 7, 70-76.
    • (1991) Parasitol. Today , vol.7 , pp. 70-76
    • Cowman, A.F.1
  • 271
    • 0025786518 scopus 로고
    • A P-glycoprotein homologue of Plasmodium falciparum is localized on the digestive vacuole
    • Cowman, A. F.; Karcz, S.; Galatis, D.; Culvenor, J. G. A P-glycoprotein homologue of Plasmodium falciparum is localized on the digestive vacuole. J. Cell Biol, 1991, 113, 1033-1042.
    • (1991) J. Cell. Biol. , vol.113 , pp. 1033-1042
    • Cowman, A.F.1    Karcz, S.2    Galatis, D.3    Culvenor, J.G.4
  • 272
    • 0025269612 scopus 로고
    • Several alleles of the multidrugresistance gene are closely linked to chloroquine resistance in Plasmodium falciparum
    • Foote, S. J.; Kyle, D. E.; Martin, R. K.; Oduola, A. M.; Forsyth, K.; Kemp, D. J.; Cowman, A. F. Several alleles of the multidrugresistance gene are closely linked to chloroquine resistance in Plasmodium falciparum. Nature, 1990, 345, 255-258.
    • (1990) Nature , vol.345 , pp. 255-258
    • Foote, S.J.1    Kyle, D.E.2    Martin, R.K.3    Oduola, A.M.4    Forsyth, K.5    Kemp, D.J.6    Cowman, A.F.7
  • 274
    • 33751211212 scopus 로고    scopus 로고
    • Quinoline-resistance reversing agents for the malaria parasite Plasmodium falciparum
    • van Schalkwyk, D. A.; Egan, T. J. Quinoline-resistance reversing agents for the malaria parasite Plasmodium falciparum. Drug Resist. Updat., 2006, 9, 211-226.
    • (2006) Drug Resist. Updat. , vol.9 , pp. 211-226
    • Van Schalkwyk, D.A.1    Egan, T.J.2
  • 276
    • 0025805723 scopus 로고
    • The chemotherapy of rodent malaria. XLVI. Reversal of mefloquine resistance in rodent Plasmodium
    • Peters, W.; Robinson, B. L. The chemotherapy of rodent malaria. XLVI. Reversal of mefloquine resistance in rodent Plasmodium. Ann. Trop. Med. Parasitol., 1991, 85, 5-10.
    • (1991) Ann. Trop. Med. Parasitol. , vol.85 , pp. 5-10
    • Peters, W.1    Robinson, B.L.2
  • 277
    • 34447323073 scopus 로고    scopus 로고
    • Energy coupling in type II topoisomerases: Why do they hydrolyze ATP?
    • Bates, A. D.; Maxwell, A. Energy coupling in type II topoisomerases: why do they hydrolyze ATP? Biochemistry, 2007, 46, 7929-7941.
    • (2007) Biochemistry , vol.46 , pp. 7929-7941
    • Bates, A.D.1    Maxwell, A.2
  • 278
    • 0022539929 scopus 로고
    • Purification and characterization of Plasmodium berghei DNA topoisomerases I and II: Drug action, inhibition of decatenation and relaxation, and stimulation of DNA cleavage
    • Riou, J. F.; Gabillot, M.; Philippe, M.; Schrevel, J.; Riou, G. Purification and characterization of Plasmodium berghei DNA topoisomerases I and II: drug action, inhibition of decatenation and relaxation, and stimulation of DNA cleavage. Biochemistry, 1986, 25, 1471-1479.
    • (1986) Biochemistry , vol.25 , pp. 1471-1479
    • Riou, J.F.1    Gabillot, M.2    Philippe, M.3    Schrevel, J.4    Riou, G.5
  • 279
    • 0029113110 scopus 로고
    • The gene encoding topoisomerase I from the human malaria parasite Plasmodium falciparum
    • Tosh, K.; Kilbey, B. The gene encoding topoisomerase I from the human malaria parasite Plasmodium falciparum. Gene, 1995, 163, 151-154.
    • (1995) Gene , vol.163 , pp. 151-154
    • Tosh, K.1    Kilbey, B.2
  • 281
    • 17444453231 scopus 로고    scopus 로고
    • Intraerythrocytic expression of topoisomerase II from Plasmodium falciparum is developmentally regulated
    • Cheesman, S.; Horrocks, P.; Tosh, K.; Kilbey, B. Intraerythrocytic expression of topoisomerase II from Plasmodium falciparum is developmentally regulated. Mol. Biochem. Parasitol., 1998, 92, 39-46.
    • (1998) Mol. Biochem. Parasitol. , vol.92 , pp. 39-46
    • Cheesman, S.1    Horrocks, P.2    Tosh, K.3    Kilbey, B.4
  • 282
    • 0032776597 scopus 로고    scopus 로고
    • Plasmodium falciparum: Stage-related expression of topoisomerase I
    • Tosh, K.; Cheesman, S.; Horrocks, P.; Kilbey, B. Plasmodium falciparum: stage-related expression of topoisomerase I. Exp. Parasitol., 1999, 91, 126-132.
    • (1999) Exp. Parasitol. , vol.91 , pp. 126-132
    • Tosh, K.1    Cheesman, S.2    Horrocks, P.3    Kilbey, B.4
  • 283
    • 0034673530 scopus 로고    scopus 로고
    • Cleavage of DNA induced by 9-anilinoacridine inhibitors of topoisomerase II in the malaria parasite Plasmodium falciparum
    • Auparakkitanon, S.; Wilairat, P. Cleavage of DNA induced by 9-anilinoacridine inhibitors of topoisomerase II in the malaria parasite Plasmodium falciparum. Biochem. Biophys. Res. Commun., 2000, 269, 406-409.
    • (2000) Biochem. Biophys. Res. Commun. , vol.269 , pp. 406-409
    • Auparakkitanon, S.1    Wilairat, P.2
  • 284
    • 43949134849 scopus 로고    scopus 로고
    • Apicoplast translation, transcription and genome replication: Targets for antimalarial antibiotics
    • Dahl, E. L.; Rosenthal, P. J. Apicoplast translation, transcription and genome replication: targets for antimalarial antibiotics. Trends Parasitol., 2008, 24, 279-284.
    • (2008) Trends Parasitol. , vol.24 , pp. 279-284
    • Dahl, E.L.1    Rosenthal, P.J.2
  • 285
    • 59049087329 scopus 로고    scopus 로고
    • Targeting the transcriptional and translational machinery of the endosymbiotic organelle in apicomplexans
    • Fleige, T.; Soldati-Favre, D. Targeting the transcriptional and translational machinery of the endosymbiotic organelle in apicomplexans. Curr. Drug. Targets, 2008, 9, 948-956.
    • (2008) Curr. Drug. Targets , vol.9 , pp. 948-956
    • Fleige, T.1    Soldati-Favre, D.2
  • 286
    • 27144449695 scopus 로고    scopus 로고
    • Designed multiple ligands. An emerging drug discovery paradigm
    • Morphy, R.; Rankovic, Z. Designed multiple ligands. An emerging drug discovery paradigm. J. Med. Chem., 2005, 48, 6523-6543.
    • (2005) J. Med. Chem. , vol.48 , pp. 6523-6543
    • Morphy, R.1    Rankovic, Z.2
  • 289
    • 34948841945 scopus 로고    scopus 로고
    • Trioxaquines and heme-artemisinin adducts inhibit the in vitro formation of hemozoin better than chloroquine
    • Loup, C.; Lelievre, J.; Benoit-Vical, F.; Meunier, B. Trioxaquines and heme-artemisinin adducts inhibit the in vitro formation of hemozoin better than chloroquine. Antimicrob. Agents Chemother., 2007, 51, 3768-3770.
    • (2007) Antimicrob. Agents Chemother. , vol.51 , pp. 3768-3770
    • Loup, C.1    Lelievre, J.2    Benoit-Vical, F.3    Meunier, B.4
  • 290
    • 71849091387 scopus 로고    scopus 로고
    • Antimalarial activities of ferroquine conjugates with either glutathione reductase inhibitors or glutathione depletors via a hydrolyzable amide linker
    • Chavain, N.; Davioud-Charvet, E.; Trivelli, X.; Mbeki, L.; Rottmann, M.; Brun, R.; Biot, C. Antimalarial activities of ferroquine conjugates with either glutathione reductase inhibitors or glutathione depletors via a hydrolyzable amide linker. Bioorg. Med. Chem., 2009, 17, 8048-8059.
    • (2009) Bioorg. Med. Chem. , vol.17 , pp. 8048-8059
    • Chavain, N.1    Davioud-Charvet, E.2    Trivelli, X.3    Mbeki, L.4    Rottmann, M.5    Brun, R.6    Biot, C.7
  • 291
    • 76749095030 scopus 로고    scopus 로고
    • Next-generation antimalarial drugs: Hybrid molecules as a new strategy in drug design
    • Muregi, F. W.; Ishih, A. Next-Generation Antimalarial Drugs: Hybrid Molecules as a New Strategy in Drug Design. Drug Develop. Res., 2010, 71, 20-32.
    • (2010) Drug Develop. Res. , vol.71 , pp. 20-32
    • Muregi, F.W.1    Ishih, A.2
  • 292
    • 19444371029 scopus 로고    scopus 로고
    • Comparative folate metabolism in humans and malaria parasites (part I): Pointers for malaria treatment from cancer chemotherapy
    • DOI 10.1016/j.pt.2005.04.002, PII S1471492205000954
    • Nzila, A.; Ward, S. A.; Marsh, K.; Sims, P. F.; Hyde, J. E. Comparative folate metabolism in humans and malaria parasites (part I): pointers for malaria treatment from cancer chemotherapy. Trends Parasitol., 2005, 21, 292-298. (Pubitemid 40726321)
    • (2005) Trends in Parasitology , vol.21 , Issue.6 , pp. 292-298
    • Nzila, A.1    Ward, S.A.2    Marsh, K.3    Sims, P.F.G.4    Hyde, J.E.5
  • 294
    • 0030829371 scopus 로고    scopus 로고
    • Variations in frequencies of drug resistance in Plasmodium falciparum
    • Rathod, P. K.; McErlean, T.; Lee, P. C. Variations in frequencies of drug resistance in Plasmodium falciparum. Proc. Natl. Acad. Sci. U. S. A., 1997, 94, 9389-9393.
    • (1997) Proc. Natl. Acad. Sci. U. S. A. , vol.94 , pp. 9389-9393
    • Rathod, P.K.1    McErlean, T.2    Lee, P.C.3
  • 295
    • 0141504172 scopus 로고    scopus 로고
    • 8-quinolinamines and their pro prodrug conjugates as potent blood-schizontocidal antimalarial agents
    • Vangapandu, S.; Sachdeva, S.; Jain, M.; Singh, S.; Singh, P. P.; Kaul, C. L.; Jain, R. 8-quinolinamines and their pro prodrug conjugates as potent blood-schizontocidal antimalarial agents. Bioorg. Med. Chem., 2003, 11, 4557-4568.
    • (2003) Bioorg. Med. Chem. , vol.11 , pp. 4557-4568
    • Vangapandu, S.1    Sachdeva, S.2    Jain, M.3    Singh, S.4    Singh, P.P.5    Kaul, C.L.6    Jain, R.7
  • 296
    • 62949126031 scopus 로고    scopus 로고
    • Macromolecular prodrugs. XII. Primaquine conjugates: Synthesis and preliminary antimalarial evaluation
    • Rajic, Z.; Kos, G.; Zorc, B.; Singh, P. P.; Singh, S. Macromolecular prodrugs. XII. Primaquine conjugates: synthesis and preliminary antimalarial evaluation. Acta Pharm., 2009, 59, 107-115.
    • (2009) Acta Pharm. , vol.59 , pp. 107-115
    • Rajic, Z.1    Kos, G.2    Zorc, B.3    Singh, P.P.4    Singh, S.5
  • 298
    • 0035090876 scopus 로고    scopus 로고
    • In vitro and in vivo antimalarial activity of ferrochloroquine, a ferrocenyl analogue of chloroquine against chloroquine-resistant malaria parasites
    • Delhaes, L.; Abessolo, H.; Biot, C.; Berry, L.; Delcourt, P.; Maciejewski, L.; Brocard, J.; Camus, D.; Dive, D. In vitro and in vivo antimalarial activity of ferrochloroquine, a ferrocenyl analogue of chloroquine against chloroquine-resistant malaria parasites. Parasitol. Res., 2001, 87, 239-244.
    • (2001) Parasitol. Res. , vol.87 , pp. 239-244
    • Delhaes, L.1    Abessolo, H.2    Biot, C.3    Berry, L.4    Delcourt, P.5    Maciejewski, L.6    Brocard, J.7    Camus, D.8    Dive, D.9
  • 299
    • 0242684594 scopus 로고    scopus 로고
    • In vitro susceptibility to a new antimalarial organometallic analogue, ferroquine, of Plasmodium falciparum isolates from the Haut-Ogooue region of Gabon
    • Atteke, C.; Ndong, J. M.; Aubouy, A.; Maciejewski, L.; Brocard, J.; Lebibi, J.; Deloron, P. In vitro susceptibility to a new antimalarial organometallic analogue, ferroquine, of Plasmodium falciparum isolates from the Haut-Ogooue region of Gabon. J. Antimicrob. Chemother., 2003, 51, 1021-1024.
    • (2003) J. Antimicrob. Chemother. , vol.51 , pp. 1021-1024
    • Atteke, C.1    Ndong, J.M.2    Aubouy, A.3    Maciejewski, L.4    Brocard, J.5    Lebibi, J.6    Deloron, P.7
  • 300
    • 78751560510 scopus 로고    scopus 로고
    • Clinical Trials.gov 2010. Dose ranging study of ferroquine with artesunate in African adults and children with uncomplicated Plasmodium falciparum malariaFARM, Accessed June, 2010
    • Clinical Trials.gov 2010]. Dose ranging study of ferroquine with artesunate in African adults and children with uncomplicated Plasmodium falciparum malaria[FARM]. http://clinicaltrials.gov/ct2/show/NCT00988507 (Accessed June, 2010).
  • 302
    • 0029161177 scopus 로고
    • Complete sequence of the mitochondrial DNA of the rhodophyte Chondrus crispus[Gigartinales]. Gene content and genome organization
    • Leblanc, C.; Boyen, C.; Richard, O.; Bonnard, G.; Grienenberger, J. M.; Kloareg, B. Complete sequence of the mitochondrial DNA of the rhodophyte Chondrus crispus[Gigartinales]. Gene content and genome organization. J. Mol. Biol., 1995, 250, 484-495.
    • (1995) J. Mol. Biol. , vol.250 , pp. 484-495
    • Leblanc, C.1    Boyen, C.2    Richard, O.3    Bonnard, G.4    Grienenberger, J.M.5    Kloareg, B.6
  • 304
    • 1842533231 scopus 로고    scopus 로고
    • Gene disruption confirms a critical role for the cysteine protease falcipain-2 in hemoglobin hydrolysis by Plasmodium falciparum
    • Sijwali, P. S.; Rosenthal, P. J. Gene disruption confirms a critical role for the cysteine protease falcipain-2 in hemoglobin hydrolysis by Plasmodium falciparum. Proc. Natl. Acad. Sci. U. S. A., 2004, 101, 4384-4389.
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 4384-4389
    • Sijwali, P.S.1    Rosenthal, P.J.2
  • 305
    • 33748328016 scopus 로고    scopus 로고
    • Gene disruptions demonstrate independent roles for the four falcipain cysteine proteases of Plasmodium falciparum
    • Sijwali, P. S.; Koo, J.; Singh, N.; Rosenthal, P. J. Gene disruptions demonstrate independent roles for the four falcipain cysteine proteases of Plasmodium falciparum. Mol. Biochem. Parasitol., 2006, 150, 96-106.
    • (2006) Mol. Biochem. Parasitol. , vol.150 , pp. 96-106
    • Sijwali, P.S.1    Koo, J.2    Singh, N.3    Rosenthal, P.J.4
  • 306
    • 0036178381 scopus 로고    scopus 로고
    • Cysteine proteases of parasitic organisms
    • Sajid, M.; McKerrow, J. H. Cysteine proteases of parasitic organisms. Mol. Biochem. Parasitol., 2002, 120, 1-21.
    • (2002) Mol. Biochem. Parasitol. , vol.120 , pp. 1-21
    • Sajid, M.1    McKerrow, J.H.2
  • 307
    • 0035112253 scopus 로고    scopus 로고
    • Comparison of efficacies of cysteine protease inhibitors against five strains of Plasmodium falciparum
    • Singh, A.; Rosenthal, P. J. Comparison of efficacies of cysteine protease inhibitors against five strains of Plasmodium falciparum. Antimicrob. Agents Chemother., 2001, 45, 949-951.
    • (2001) Antimicrob. Agents Chemother. , vol.45 , pp. 949-951
    • Singh, A.1    Rosenthal, P.J.2
  • 308
    • 0027512171 scopus 로고
    • Inhibition of a Plasmodium vinckei cysteine proteinase cures murine malaria
    • Rosenthal, P. J.; Lee, G. K.; Smith, R. E. Inhibition of a Plasmodium vinckei cysteine proteinase cures murine malaria. J. Clin. Invest., 1993, 91, 1052-1056.
    • (1993) J. Clin. Invest. , vol.91 , pp. 1052-1056
    • Rosenthal, P.J.1    Lee, G.K.2    Smith, R.E.3
  • 309
    • 0024208917 scopus 로고
    • A malarial cysteine proteinase is necessary for hemoglobin degradation by Plasmodium falciparum
    • Rosenthal, P. J.; McKerrow, J. H.; Aikawa, M.; Nagasawa, H.; Leech, J. H. A malarial cysteine proteinase is necessary for hemoglobin degradation by Plasmodium falciparum. J. Clin. Invest., 1988, 82, 1560-1566.
    • (1988) J. Clin. Invest. , vol.82 , pp. 1560-1566
    • Rosenthal, P.J.1    McKerrow, J.H.2    Aikawa, M.3    Nagasawa, H.4    Leech, J.H.5
  • 311
    • 0025719869 scopus 로고
    • Antimalarial effects of peptide inhibitors of a Plasmodium falciparum cysteine proteinase
    • Rosenthal, P. J.; Wollish, W. S.; Palmer, J. T.; Rasnick, D. Antimalarial effects of peptide inhibitors of a Plasmodium falciparum cysteine proteinase. J. Clin. Invest., 1991, 88, 1467-1472.
    • (1991) J. Clin. Invest. , vol.88 , pp. 1467-1472
    • Rosenthal, P.J.1    Wollish, W.S.2    Palmer, J.T.3    Rasnick, D.4
  • 313
  • 314
    • 0035985069 scopus 로고    scopus 로고
    • Stage-specific antimalarial activity of cysteine protease inhibitors
    • Shenai, B. R.; Semenov, A. V.; Rosenthal, P. J. Stage-specific antimalarial activity of cysteine protease inhibitors. Biol. Chem., 2002, 383, 843-847.
    • (2002) Biol. Chem. , vol.383 , pp. 843-847
    • Shenai, B.R.1    Semenov, A.V.2    Rosenthal, P.J.3
  • 315
    • 0141509925 scopus 로고    scopus 로고
    • Selective inhibition of a two-step egress of malaria parasites from the host erythrocyte
    • Wickham, M. E.; Culvenor, J. G.; Cowman, A. F. Selective inhibition of a two-step egress of malaria parasites from the host erythrocyte. J. Biol. Chem., 2003, 278, 37658-37663.
    • (2003) J. Biol. Chem. , vol.278 , pp. 37658-37663
    • Wickham, M.E.1    Culvenor, J.G.2    Cowman, A.F.3
  • 316
    • 0035793051 scopus 로고    scopus 로고
    • Malaria parasite exit from the host erythrocyte: A two-step process requiring extraerythrocytic proteolysis
    • Salmon, B. L.; Oksman, A.; Goldberg, D. E. Malaria parasite exit from the host erythrocyte: a two-step process requiring extraerythrocytic proteolysis. Proc. Natl. Acad. Sci. U. S. A., 2001, 98, 271-276.
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 271-276
    • Salmon, B.L.1    Oksman, A.2    Goldberg, D.E.3
  • 317
    • 65749094248 scopus 로고    scopus 로고
    • Artemisinin-dipeptidyl vinyl sulfone hybrid molecules: Design, synthesis and preliminary SAR for antiplasmodial activity and falcipain-2 inhibition
    • Capela, R.; Oliveira, R.; Goncalves, L. M.; Domingos, A.; Gut, J.; Rosenthal, P. J.; Lopes, F.; Moreira, R. Artemisinin-dipeptidyl vinyl sulfone hybrid molecules: design, synthesis and preliminary SAR for antiplasmodial activity and falcipain-2 inhibition. Bioorg. Med. Chem. Lett., 2009, 19, 3229-3232.
    • (2009) Bioorg. Med. Chem. Lett. , vol.19 , pp. 3229-3232
    • Capela, R.1    Oliveira, R.2    Goncalves, L.M.3    Domingos, A.4    Gut, J.5    Rosenthal, P.J.6    Lopes, F.7    Moreira, R.8
  • 318
    • 16244370734 scopus 로고    scopus 로고
    • Design, synthesis and anti-plasmodial evaluation in vitro of new 4-aminoquinoline isatin derivatives
    • Chiyanzu, I.; Clarkson, C.; Smith, P. J.; Lehman, J.; Gut, J.; Rosenthal, P. J.; Chibale, K. Design, synthesis and anti-plasmodial evaluation in vitro of new 4-aminoquinoline isatin derivatives. Bioorg. Med. Chem., 2005, 13, 3249-3261.
    • (2005) Bioorg. Med. Chem. , vol.13 , pp. 3249-3261
    • Chiyanzu, I.1    Clarkson, C.2    Smith, P.J.3    Lehman, J.4    Gut, J.5    Rosenthal, P.J.6    Chibale, K.7
  • 319
    • 0031574219 scopus 로고    scopus 로고
    • The malaria parasite supplies glutathione to its host cell-investigation of glutathione transport and metabolism in human erythrocytes infected with Plasmodium falciparum
    • Atamna, H.; Ginsburg, H. The malaria parasite supplies glutathione to its host cell-investigation of glutathione transport and metabolism in human erythrocytes infected with Plasmodium falciparum. Eur. J. Biochem., 1997, 250, 670-679.
    • (1997) Eur. J. Biochem. , vol.250 , pp. 670-679
    • Atamna, H.1    Ginsburg, H.2
  • 320
    • 47749090916 scopus 로고    scopus 로고
    • The aza-analogues of 1, 4-naphthoquinones are potent substrates and inhibitors of plasmodial thioredoxin and glutathione reductases and of human erythrocyte glutathione reductase
    • Morin, C.; Besset, T.; Moutet, J. C.; Fayolle, M.; Bruckner, M.; Limosin, D.; Becker, K.; Davioud-Charvet, E. The aza-analogues of 1, 4-naphthoquinones are potent substrates and inhibitors of plasmodial thioredoxin and glutathione reductases and of human erythrocyte glutathione reductase. Org. Biomol. Chem., 2008, 6, 2731-2742.
    • (2008) Org. Biomol. Chem. , vol.6 , pp. 2731-2742
    • Morin, C.1    Besset, T.2    Moutet, J.C.3    Fayolle, M.4    Bruckner, M.5    Limosin, D.6    Becker, K.7    Davioud-Charvet, E.8
  • 321
    • 0346398299 scopus 로고    scopus 로고
    • Doubledrug development against antioxidant enzymes from Plasmodium falciparum
    • Biot, C.; Dessolin, J.; Grellier, P.; Davioud-Charvet, E. Doubledrug development against antioxidant enzymes from Plasmodium falciparum. Redox Rep., 2003, 8, 280-283.
    • (2003) Redox Rep. , vol.8 , pp. 280-283
    • Biot, C.1    Dessolin, J.2    Grellier, P.3    Davioud-Charvet, E.4
  • 322
    • 30144444156 scopus 로고    scopus 로고
    • Glutathione S-transferase from malarial parasites: Structural and functional aspects
    • Deponte, M.; Becker, K. Glutathione S-transferase from malarial parasites: structural and functional aspects. Methods Enzymol., 2005, 401, 241-253.
    • (2005) Methods Enzymol. , vol.401 , pp. 241-253
    • Deponte, M.1    Becker, K.2
  • 327
    • 0027165195 scopus 로고
    • Control of heme polymerase by chloroquine and other quinoline derivatives
    • Chou, A. C.; Fitch, C. D. Control of heme polymerase by chloroquine and other quinoline derivatives. Biochem. Biophys. Res. Commun., 1993, 195, 422-427.
    • (1993) Biochem. Biophys. Res. Commun. , vol.195 , pp. 422-427
    • Chou, A.C.1    Fitch, C.D.2
  • 328
    • 0032520664 scopus 로고    scopus 로고
    • An assessment of drug-haematin binding as a mechanism for inhibition of haematin polymerisation by quinoline antimalarials
    • Dorn, A.; Vippagunta, S. R.; Matile, H.; Jaquet, C.; Vennerstrom, J. L.; Ridley, R. G. An assessment of drug-haematin binding as a mechanism for inhibition of haematin polymerisation by quinoline antimalarials. Biochem. Pharmacol., 1998, 55, 727-736.
    • (1998) Biochem. Pharmacol. , vol.55 , pp. 727-736
    • Dorn, A.1    Vippagunta, S.R.2    Matile, H.3    Jaquet, C.4    Vennerstrom, J.L.5    Ridley, R.G.6
  • 331
    • 0028360131 scopus 로고
    • Synthesis and in vitro evaluation of 9-anilino-3, 6-diaminoacridines active against a multidrug-resistant strain of the malaria parasite Plasmodium falciparum
    • Gamage, S. A.; Tepsiri, N.; Wilairat, P.; Wojcik, S. J.; Figgitt, D. P.; Ralph, R. K.; Denny, W. A. Synthesis and in vitro evaluation of 9-anilino-3, 6-diaminoacridines active against a multidrug-resistant strain of the malaria parasite Plasmodium falciparum. J. Med. Chem., 1994, 37, 1486-1494.
    • (1994) J. Med. Chem. , vol.37 , pp. 1486-1494
    • Gamage, S.A.1    Tepsiri, N.2    Wilairat, P.3    Wojcik, S.J.4    Figgitt, D.P.5    Ralph, R.K.6    Denny, W.A.7
  • 332
    • 0034805433 scopus 로고    scopus 로고
    • Plasmodium falciparum: The effects of atovaquone resistance on respiration
    • Suswam, E.; Kyle, D.; Lang-Unnasch, N. Plasmodium falciparum: the effects of atovaquone resistance on respiration. Exp. Parasitol., 2001, 98, 180-187.
    • (2001) Exp. Parasitol. , vol.98 , pp. 180-187
    • Suswam, E.1    Kyle, D.2    Lang-Unnasch, N.3
  • 333
    • 24144482399 scopus 로고    scopus 로고
    • A post-genomic view of the mitochondrion in malaria parasites
    • Vaidya, A. B.; Mather, M. W. A post-genomic view of the mitochondrion in malaria parasites. Curr. Top. Microbiol. Immunol., 2005, 295, 233-250.
    • (2005) Curr. Top. Microbiol. Immunol. , vol.295 , pp. 233-250
    • Vaidya, A.B.1    Mather, M.W.2
  • 336
    • 0027537795 scopus 로고
    • Structure-activity relationships and modes of action of 9-anilinoacridines against chloroquine-resistant Plasmodium falciparum in vitro
    • Chavalitshewinkoon, P.; Wilairat, P.; Gamage, S.; Denny, W.; Figgitt, D.; Ralph, R. Structure-activity relationships and modes of action of 9-anilinoacridines against chloroquine-resistant Plasmodium falciparum in vitro. Antimicrob. Agents Chemother., 1993, 37, 403-406.
    • (1993) Antimicrob. Agents Chemother. , vol.37 , pp. 403-406
    • Chavalitshewinkoon, P.1    Wilairat, P.2    Gamage, S.3    Denny, W.4    Figgitt, D.5    Ralph, R.6
  • 337
    • 77952303346 scopus 로고    scopus 로고
    • Efficacy and safety of a fixed-dose oral combination of pyronaridineartesunate compared with artemether-lumefantrine in children and adults with uncomplicated Plasmodium falciparum malaria: A randomised non-inferiority trial
    • Tshefu, A. K.; Gaye, O.; Kayentao, K.; Thompson, R.; Bhatt, K. M.; Sesay, S. S.; Bustos, D. G.; Tjitra, E.; Bedu-Addo, G.; Borghini-Fuhrer, I.; Duparc, S.; Shin, C. S.; Fleckenstein, L. Efficacy and safety of a fixed-dose oral combination of pyronaridineartesunate compared with artemether-lumefantrine in children and adults with uncomplicated Plasmodium falciparum malaria: a randomised non-inferiority trial. Lancet, 2010, 375, 1457-1467.
    • (2010) Lancet , vol.375 , pp. 1457-1467
    • Tshefu, A.K.1    Gaye, O.2    Kayentao, K.3    Thompson, R.4    Bhatt, K.M.5    Sesay, S.S.6    Bustos, D.G.7    Tjitra, E.8    Bedu-Addo, G.9    Borghini-Fuhrer, I.10    Duparc, S.11    Shin, C.S.12    Fleckenstein, L.13
  • 338
    • 67349124872 scopus 로고    scopus 로고
    • The global portfolio of new antimalarial medicines under development
    • Olliaro, P.; Wells, T. N. The global portfolio of new antimalarial medicines under development. Clin. Pharmacol. Ther., 2009, 85, 584-595.
    • (2009) Clin. Pharmacol. Ther. , vol.85 , pp. 584-595
    • Olliaro, P.1    Wells, T.N.2
  • 342
    • 58249143778 scopus 로고    scopus 로고
    • Accumulation of artemisinin trioxane derivatives within neutral lipids of Plasmodium falciparum malaria parasites is endoperoxide-dependent
    • Hartwig, C. L.; Rosenthal, A. S.; D'Angelo, J.; Griffin, C. E.; Posner, G. H.; Cooper, R. A. Accumulation of artemisinin trioxane derivatives within neutral lipids of Plasmodium falciparum malaria parasites is endoperoxide-dependent. Biochem. Pharmacol., 2009, 77, 322-336.
    • (2009) Biochem. Pharmacol. , vol.77 , pp. 322-336
    • Hartwig, C.L.1    Rosenthal, A.S.2    D'Angelo, J.3    Griffin, C.E.4    Posner, G.H.5    Cooper, R.A.6
  • 345
    • 17144422120 scopus 로고    scopus 로고
    • Defining the role of PfCRT in Plasmodium falciparum chloroquine resistance
    • Bray, P. G.; Martin, R. E.; Tilley, L.; Ward, S. A.; Kirk, K.; Fidock, D. A. Defining the role of PfCRT in Plasmodium falciparum chloroquine resistance. Mol. Microbiol., 2005, 56, 323-333.
    • (2005) Mol. Microbiol. , vol.56 , pp. 323-333
    • Bray, P.G.1    Martin, R.E.2    Tilley, L.3    Ward, S.A.4    Kirk, K.5    Fidock, D.A.6
  • 346
    • 0023472424 scopus 로고
    • Trypanosoma cruzi: Differentiation to metacyclic trypomastigotes in the presence of ADP-ribosyltransferase inhibitors
    • Isola, E. L.; Lammel, E. M.; Gonzalez Cappa, S. M. Trypanosoma cruzi: differentiation to metacyclic trypomastigotes in the presence of ADP-ribosyltransferase inhibitors. Exp. Parasitol., 1987, 64, 424-429.
    • (1987) Exp. Parasitol. , vol.64 , pp. 424-429
    • Isola, E.L.1    Lammel, E.M.2    Gonzalez Cappa, S.M.3
  • 347
    • 0035400271 scopus 로고    scopus 로고
    • Characterization of poly[ADP-ribose]polymerase from Crithidia fasciculata: Enzyme inhibition by beta-lapachone
    • Villamil, S. F.; Podesta, D.; Molina Portela, M. D.; Stoppani, A. Characterization of poly[ADP-ribose]polymerase from Crithidia fasciculata: enzyme inhibition by beta-lapachone. Mol. Biochem. Parasitol., 2001, 115, 249-256.
    • (2001) Mol. Biochem. Parasitol. , vol.115 , pp. 249-256
    • Villamil, S.F.1    Podesta, D.2    Molina Portela, M.D.3    Stoppani, A.4
  • 348
    • 0028572388 scopus 로고
    • Effect of 6[5H]-phenanthridinone, an inhibitor of poly (ADP-ribose) polymerase, on cultured tumor cells
    • Weltin, D.; Marchal, J.; Dufour, P.; Potworowski, E.; Oth, D.; Bischoff, P. Effect of 6[5H]-phenanthridinone, an inhibitor of poly (ADP-ribose) polymerase, on cultured tumor cells. Oncol. Res., 1994, 6, 399-403.
    • (1994) Oncol. Res. , vol.6 , pp. 399-403
    • Weltin, D.1    Marchal, J.2    Dufour, P.3    Potworowski, E.4    Oth, D.5    Bischoff, P.6
  • 349
    • 0029089917 scopus 로고
    • Potential chemotherapeutic activity of 4-iodo-3-nitrobenzamide. Metabolic reduction to the 3-nitroso derivative and induction of cell death in tumor cells in culture
    • Mendeleyev, J.; Kirsten, E.; Hakam, A.; Buki, K. G.; Kun, E. Potential chemotherapeutic activity of 4-iodo-3-nitrobenzamide. Metabolic reduction to the 3-nitroso derivative and induction of cell death in tumor cells in culture. Biochem. Pharmacol., 1995, 50, 705-714.
    • (1995) Biochem. Pharmacol. , vol.50 , pp. 705-714
    • Mendeleyev, J.1    Kirsten, E.2    Hakam, A.3    Buki, K.G.4    Kun, E.5
  • 350
    • 0031762817 scopus 로고    scopus 로고
    • Potentiation of anti-cancer agent cytotoxicity by the potent poly (ADP-ribose) polymerase inhibitors NU1025 and NU1064
    • Bowman, K. J.; White, A.; Golding, B. T.; Griffin, R. J.; Curtin, N. J. Potentiation of anti-cancer agent cytotoxicity by the potent poly (ADP-ribose) polymerase inhibitors NU1025 and NU1064. Br. J. Cancer, 1998, 78, 1269-1277.
    • (1998) Br. J. Cancer , vol.78 , pp. 1269-1277
    • Bowman, K.J.1    White, A.2    Golding, B.T.3    Griffin, R.J.4    Curtin, N.J.5
  • 351
    • 0037085761 scopus 로고    scopus 로고
    • Combined treatment with temozolomide and poly (ADP-ribose) polymerase inhibitor enhances survival of mice bearing hematologic malignancy at the central nervous system site
    • Tentori, L.; Leonetti, C.; Scarsella, M.; d'Amati, G.; Portarena, I.; Zupi, G.; Bonmassar, E.; Graziani, G. Combined treatment with temozolomide and poly (ADP-ribose) polymerase inhibitor enhances survival of mice bearing hematologic malignancy at the central nervous system site. Blood, 2002, 99, 2241-2244.
    • (2002) Blood , vol.99 , pp. 2241-2244
    • Tentori, L.1    Leonetti, C.2    Scarsella, M.3    D'Amati, G.4    Portarena, I.5    Zupi, G.6    Bonmassar, E.7    Graziani, G.8
  • 353
    • 0035029463 scopus 로고    scopus 로고
    • Enhanced polyadenosine diphosphate-ribosylation in cirrhotic liver and carcinoma tissues in patients with hepatocellular carcinoma
    • Shiobara, M.; Miyazaki, M.; Ito, H.; Togawa, A.; Nakajima, N.; Nomura, F.; Morinaga, N.; Noda, M. Enhanced polyadenosine diphosphate-ribosylation in cirrhotic liver and carcinoma tissues in patients with hepatocellular carcinoma. J. Gastroenterol. Hepatol., 2001, 16, 338-344.
    • (2001) J. Gastroenterol. Hepatol. , vol.16 , pp. 338-344
    • Shiobara, M.1    Miyazaki, M.2    Ito, H.3    Togawa, A.4    Nakajima, N.5    Nomura, F.6    Morinaga, N.7    Noda, M.8
  • 357
    • 33749034730 scopus 로고    scopus 로고
    • Topoisomerase I inhibitors: Camptothecins and beyond
    • Pommier, Y. Topoisomerase I inhibitors: camptothecins and beyond. Nat. Rev. Cancer, 2006, 6, 789-802.
    • (2006) Nat. Rev. Cancer , vol.6 , pp. 789-802
    • Pommier, Y.1
  • 358
    • 18844479929 scopus 로고    scopus 로고
    • Effects of camptothecin, a topoisomerase I inhibitor, on Plasmodium falciparum
    • Bodley, A. L.; Cumming, J. N.; Shapiro, T. A. Effects of camptothecin, a topoisomerase I inhibitor, on Plasmodium falciparum. Biochem. Pharmacol., 1998, 55, 709-711.
    • (1998) Biochem. Pharmacol. , vol.55 , pp. 709-711
    • Bodley, A.L.1    Cumming, J.N.2    Shapiro, T.A.3
  • 359
    • 0028694108 scopus 로고
    • Mechanisms of resistance to topoisomerase inhibitors
    • Chen, A. Y.; Liu, L. F. Mechanisms of resistance to topoisomerase inhibitors. Cancer Treat. Res., 1994, 73, 263-281.
    • (1994) Cancer Treat. Res. , vol.73 , pp. 263-281
    • Chen, A.Y.1    Liu, L.F.2
  • 360
    • 33646263371 scopus 로고    scopus 로고
    • Evidence on the chromosomal location of centromeric DNA in Plasmodium falciparum from etoposide-mediated topoisomerase-II cleavage
    • Kelly, J. M.; McRobert, L.; Baker, D. A. Evidence on the chromosomal location of centromeric DNA in Plasmodium falciparum from etoposide-mediated topoisomerase-II cleavage. Proc. Natl. Acad. Sci. U. S. A., 2006, 103, 6706-6711.
    • (2006) Proc. Natl. Acad. Sci. U. S. A. , vol.103 , pp. 6706-6711
    • Kelly, J.M.1    McRobert, L.2    Baker, D.A.3
  • 361
    • 0026546254 scopus 로고
    • Relative activity of structural analogues of amsacrine against human leukemia cell lines containing amsacrine-sensitive or-resistant forms of topoisomerase II: Use of computer simulations in new drug development
    • Zwelling, L. A.; Mitchell, M. J.; Satitpunwaycha, P.; Mayes, J.; Altschuler, E.; Hinds, M.; Baguley, B. C. Relative activity of structural analogues of amsacrine against human leukemia cell lines containing amsacrine-sensitive or-resistant forms of topoisomerase II: use of computer simulations in new drug development. Cancer Res., 1992, 52, 209-217.
    • (1992) Cancer Res. , vol.52 , pp. 209-217
    • Zwelling, L.A.1    Mitchell, M.J.2    Satitpunwaycha, P.3    Mayes, J.4    Altschuler, E.5    Hinds, M.6    Baguley, B.C.7
  • 362
    • 0034620614 scopus 로고    scopus 로고
    • Gametocytocidal activity of pyronaridine and DNA topoisomerase II inhibitors against multidrug-resistant Plasmodium falciparum in vitro
    • Chavalitshewinkoon-Petmitr, P.; Pongvilairat, G.; Auparakkitanon, S.; Wilairat, P. Gametocytocidal activity of pyronaridine and DNA topoisomerase II inhibitors against multidrug-resistant Plasmodium falciparum in vitro. Parasitol. Int., 2000, 48, 275-280.
    • (2000) Parasitol. Int. , vol.48 , pp. 275-280
    • Chavalitshewinkoon-Petmitr, P.1    Pongvilairat, G.2    Auparakkitanon, S.3    Wilairat, P.4
  • 363
    • 0026095986 scopus 로고
    • Pyronaridine: A new antimalarial drug
    • Fu, S.; Xiao, S. H. Pyronaridine: A new antimalarial drug. Parasitol. Today, 1991, 7, 310-313.
    • (1991) Parasitol. Today , vol.7 , pp. 310-313
    • Fu, S.1    Xiao, S.H.2
  • 367
    • 0036142318 scopus 로고    scopus 로고
    • The antimalarial and cytotoxic drug cryptolepine intercalates into DNA at cytosine-cytosine sites
    • Lisgarten, J. N.; Coll, M.; Portugal, J.; Wright, C. W.; Aymami, J. The antimalarial and cytotoxic drug cryptolepine intercalates into DNA at cytosine-cytosine sites. Nat. Struct. Biol., 2002, 9, 57-60.
    • (2002) Nat. Struct. Biol. , vol.9 , pp. 57-60
    • Lisgarten, J.N.1    Coll, M.2    Portugal, J.3    Wright, C.W.4    Aymami, J.5
  • 368
    • 0035866694 scopus 로고    scopus 로고
    • New synthesis of benzo-delta-carbolines, cryptolepines, and their salts: In vitro cytotoxic, antiplasmodial, and antitrypanosomal activities of delta-carbolines, benzo-delta-carbolines, and cryptolepines
    • Arzel, E.; Rocca, P.; Grellier, P.; Labaeid, M.; Frappier, F.; Gueritte, F.; Gaspard, C.; Marsais, F.; Godard, A.; Queguiner, G. New synthesis of benzo-delta-carbolines, cryptolepines, and their salts: in vitro cytotoxic, antiplasmodial, and antitrypanosomal activities of delta-carbolines, benzo-delta-carbolines, and cryptolepines. J. Med. Chem., 2001, 44, 949-960.
    • (2001) J. Med. Chem. , vol.44 , pp. 949-960
    • Arzel, E.1    Rocca, P.2    Grellier, P.3    Labaeid, M.4    Frappier, F.5    Gueritte, F.6    Gaspard, C.7    Marsais, F.8    Godard, A.9    Queguiner, G.10
  • 372
    • 0022374762 scopus 로고
    • The fluoroquinolones: Pharmacology, clinical uses, and toxicities in humans
    • Hooper, D. C.; Wolfson, J. S. The fluoroquinolones: pharmacology, clinical uses, and toxicities in humans. Antimicrob. Agents Chemother., 1985, 28, 716-721.
    • (1985) Antimicrob. Agents Chemother. , vol.28 , pp. 716-721
    • Hooper, D.C.1    Wolfson, J.S.2
  • 373
    • 0032856370 scopus 로고    scopus 로고
    • Mechanism of fluoroquinolone action
    • Drlica, K. Mechanism of fluoroquinolone action. Curr. Opin. Microbiol., 1999, 2, 504-508.
    • (1999) Curr. Opin. Microbiol. , vol.2 , pp. 504-508
    • Drlica, K.1
  • 374
    • 0022359647 scopus 로고
    • The fluoroquinolones: Structures, mechanisms of action and resistance, and spectra of activity in vitro
    • Wolfson, J. S.; Hooper, D. C. The fluoroquinolones: structures, mechanisms of action and resistance, and spectra of activity in vitro. Antimicrob. Agents Chemother., 1985, 28, 581-586.
    • (1985) Antimicrob. Agents Chemother. , vol.28 , pp. 581-586
    • Wolfson, J.S.1    Hooper, D.C.2
  • 377
    • 33646453477 scopus 로고    scopus 로고
    • New potential antimalarial agents: Therapeutic-index evaluation of pyrroloquinazolinediamine and its prodrugs in a rat model of severe malaria
    • Xie, L. H.; Li, Q.; Lin, A. J.; Smith, K.; Zhang, J.; Skillman, D. S. New potential antimalarial agents: therapeutic-index evaluation of pyrroloquinazolinediamine and its prodrugs in a rat model of severe malaria. Antimicrob. Agents Chemother., 2006, 50, 1649-1655.
    • (2006) Antimicrob. Agents Chemother. , vol.50 , pp. 1649-1655
    • Xie, L.H.1    Li, Q.2    Lin, A.J.3    Smith, K.4    Zhang, J.5    Skillman, D.S.6
  • 378
    • 53049083866 scopus 로고    scopus 로고
    • Plasmodium berghei: Lack of antimalarial activity of an analogue of folate precursor, 2, 4-diamino-6-hydroxymethylpteridine in a mouse model
    • Muregi, F. W.; Kino, H.; Ishih, A. Plasmodium berghei: lack of antimalarial activity of an analogue of folate precursor, 2, 4-diamino-6-hydroxymethylpteridine in a mouse model. Exp. Parasitol., 2008, 120, 286-289.
    • (2008) Exp. Parasitol. , vol.120 , pp. 286-289
    • Muregi, F.W.1    Kino, H.2    Ishih, A.3
  • 379
    • 0025760770 scopus 로고
    • Pyrimethamin-resistant Plasmodium falciparum lack crossresistance to methotrexate and 2,4-diamino-5-[substituted benzyl]pyrimidines
    • Walter, R. D.; Bergmann, B.; Kansy, M.; Wiese, M.; Seydel, J. K. Pyrimethamin-resistant Plasmodium falciparum lack crossresistance to methotrexate and 2,4-diamino-5-[substituted benzyl]pyrimidines. Parasitol. Res., 1991, 77, 346-350.
    • (1991) Parasitol. Res. , vol.77 , pp. 346-350
    • Walter, R.D.1    Bergmann, B.2    Kansy, M.3    Wiese, M.4    Seydel, J.K.5
  • 380
    • 0019821777 scopus 로고
    • Plasmodium falciparum: In vitro induction of resistance to aminopterin
    • Golenser, J.; Casuto, D.; Pollack, Y. Plasmodium falciparum: in vitro induction of resistance to aminopterin. Exp. Parasitol., 1981, 52, 371-377.
    • (1981) Exp. Parasitol. , vol.52 , pp. 371-377
    • Golenser, J.1    Casuto, D.2    Pollack, Y.3
  • 381
    • 42049115684 scopus 로고    scopus 로고
    • Effect of folate derivatives on the activity of antifolate drugs used against malaria and cancer
    • Nduati, E.; Diriye, A.; Ommeh, S.; Mwai, L.; Kiara, S.; Masseno, V.; Kokwaro, G.; Nzila, A. Effect of folate derivatives on the activity of antifolate drugs used against malaria and cancer. Parasitol. Res., 2008, 102, 1227-1234.
    • (2008) Parasitol. Res. , vol.102 , pp. 1227-1234
    • Nduati, E.1    Diriye, A.2    Ommeh, S.3    Mwai, L.4    Kiara, S.5    Masseno, V.6    Kokwaro, G.7    Nzila, A.8
  • 382
    • 24144466520 scopus 로고    scopus 로고
    • 2, 4-diaminopteridine-based compounds as precursors for de novo synthesis of antifolates: A novel class of antimalarials
    • Nduati, E.; Hunt, S.; Kamau, E. M.; Nzila, A. 2, 4-diaminopteridine-based compounds as precursors for de novo synthesis of antifolates: a novel class of antimalarials. Antimicrob. Agents Chemother., 2005, 49, 3652-3657.
    • (2005) Antimicrob. Agents Chemother. , vol.49 , pp. 3652-3657
    • Nduati, E.1    Hunt, S.2    Kamau, E.M.3    Nzila, A.4
  • 383
    • 68949187952 scopus 로고    scopus 로고
    • Methotrexate and aminopterin lack in vivo antimalarial activity against murine malaria species
    • Irungu, B.; Kiboi, D.; Langat, B.; Rukunga, G.; Wittlin, S.; Nzila, A. Methotrexate and aminopterin lack in vivo antimalarial activity against murine malaria species. Exp. Parasitol., 2009, 123, 118-121.
    • (2009) Exp. Parasitol. , vol.123 , pp. 118-121
    • Irungu, B.1    Kiboi, D.2    Langat, B.3    Rukunga, G.4    Wittlin, S.5    Nzila, A.6


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