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Volumn 56, Issue 13, 2013, Pages 5231-5246

Quinoline drug-heme interactions and implications for antimalarial cytostatic versus cytocidal activities

Author keywords

[No Author keywords available]

Indexed keywords

AMODIAQUINE; ANTIMALARIAL AGENT; ARTEMETHER; ARTEMISININ; ARTESUNATE; ATOVAQUONE; BENFLUMETOL; CHLOROQUINE; DIHYDROARTEMISININ; HALOFANTRINE; HEME; HEMOGLOBIN; HEMOZOIN; MEFLOQUINE; PIPERAQUINE; PRIMAQUINE; PYRIMETHAMINE; QUINIDINE; QUININE; QUINOLINE; SULFADOXINE;

EID: 84880161070     PISSN: 00222623     EISSN: 15204804     Source Type: Journal    
DOI: 10.1021/jm400282d     Document Type: Article
Times cited : (160)

References (183)
  • 1
    • 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
  • 2
    • 77954309291 scopus 로고    scopus 로고
    • Quinolines and Structurally Related Heterocycles as Antimalarials
    • Kaur, K.; Jain, M.; Reddy, R. P.; Jain, R. Quinolines and Structurally Related Heterocycles as Antimalarials Eur. J. Med. Chem. 2010, 45, 3245-3264
    • (2010) Eur. J. Med. Chem. , vol.45 , pp. 3245-3264
    • Kaur, K.1    Jain, M.2    Reddy, R.P.3    Jain, R.4
  • 3
    • 66949146530 scopus 로고    scopus 로고
    • Molecular and Physiologic Basis of Quinoline Drug Resistance in Plasmodium falciparum Malaria
    • Roepe, P. D. Molecular and Physiologic Basis of Quinoline Drug Resistance in Plasmodium falciparum Malaria Future Microbiol. 2009, 4, 441-455
    • (2009) Future Microbiol. , vol.4 , pp. 441-455
    • Roepe, P.D.1
  • 6
    • 33947445299 scopus 로고
    • Aminoalkylphenols as Antimalarials. II. (Heterocyclic-amino)-α- amino- o -cresols. The Synthesis of Camoquin
    • Burckhalter, J. H.; Tendick, F. H.; Jones, E. M.; Jones, P. A.; Holcomb, W. F.; Rawlins, A. L. Aminoalkylphenols as Antimalarials. II. (Heterocyclic-amino)-α-amino- o -cresols. The Synthesis of Camoquin J. Am. Chem. Soc. 1948, 70, 1363-1373
    • (1948) J. Am. Chem. Soc. , vol.70 , pp. 1363-1373
    • Burckhalter, J.H.1    Tendick, F.H.2    Jones, E.M.3    Jones, P.A.4    Holcomb, W.F.5    Rawlins, A.L.6
  • 8
    • 79952193925 scopus 로고    scopus 로고
    • World Health Organization (WHO): Geneva, Switzerland
    • World Malaria Report 2010; World Health Organization (WHO): Geneva, Switzerland, 2010; http://www.who.int/malaria/publications/atoz/9789241564106/ en/index.html.
    • (2010) World Malaria Report 2010
  • 9
    • 27944483714 scopus 로고    scopus 로고
    • Antimalarial Drug Synergism and Antagonism: Mechanistic and Clinical Significance
    • Bell, A. Antimalarial Drug Synergism and Antagonism: Mechanistic and Clinical Significance FEMS Microbiol. Lett. 2005, 253, 171-184
    • (2005) FEMS Microbiol. Lett. , vol.253 , pp. 171-184
    • Bell, A.1
  • 10
    • 84857735297 scopus 로고    scopus 로고
    • Reversed Chloroquine Molecules as a Strategy to Overcome Resistance in Malaria
    • Peyton, D. H. Reversed Chloroquine Molecules as a Strategy To Overcome Resistance in Malaria Curr. Top. Med. Chem. 2012, 12, 400-407
    • (2012) Curr. Top. Med. Chem. , vol.12 , pp. 400-407
    • Peyton, D.H.1
  • 11
    • 0037154180 scopus 로고    scopus 로고
    • Four Plasmepsins Are Active in the Plasmodium falciparum Food Vacuole, Including a Protease with an Active-Site Histidine
    • Banerjee, R.; Liu, J.; Beatty, W.; Pelosof, L.; Klemba, M.; Goldberg, D. E. Four Plasmepsins Are Active in the Plasmodium falciparum Food Vacuole, Including a Protease with an Active-Site Histidine Proc. Natl. Acad. Sci. U.S.A. 2002, 99, 990-995
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 990-995
    • Banerjee, R.1    Liu, J.2    Beatty, W.3    Pelosof, L.4    Klemba, M.5    Goldberg, D.E.6
  • 12
    • 0001402353 scopus 로고    scopus 로고
    • Cysteine Proteinase Inhibitors Block Early Steps in Hemoglobin Degradation by Cultured Malaria Parasites
    • Gamboa de Domínguez, N. D.; Rosenthal, P. J. Cysteine Proteinase Inhibitors Block Early Steps in Hemoglobin Degradation by Cultured Malaria Parasites Blood 1996, 87, 4448-4454
    • (1996) Blood , vol.87 , pp. 4448-4454
    • Gamboa De Domínguez, N.D.1    Rosenthal, P.J.2
  • 13
    • 0033560719 scopus 로고    scopus 로고
    • Inhibition of the Peroxidative Degradation of Haem as the Basis of Action of Chloroquine and Other Quinoline Antimalarials
    • Loria, P.; Miller, S.; Foley, M.; Tilley, L. Inhibition of the Peroxidative Degradation of Haem as the Basis of Action of Chloroquine and Other Quinoline Antimalarials Biochem. J. 1999, 339, 363-370
    • (1999) Biochem. J. , vol.339 , pp. 363-370
    • Loria, P.1    Miller, S.2    Foley, M.3    Tilley, L.4
  • 15
    • 0033732757 scopus 로고    scopus 로고
    • Mechanism of Heme Degradation by Heme Oxygenase
    • Yoshida, T.; Migita, T. C. Mechanism of Heme Degradation by Heme Oxygenase J. Inorg. Biochem. 2000, 82, 33-41
    • (2000) J. Inorg. Biochem. , vol.82 , pp. 33-41
    • Yoshida, T.1    Migita, T.C.2
  • 17
    • 4744364660 scopus 로고    scopus 로고
    • Food Vacuole-Associated Lipid Bodies and Heterogeneous Lipid Environments in the Malaria Parasite Plasmodium falciparum
    • Jackson, K. E.; Klonis, N.; Ferguson, D. J.; Adisa, A.; Dogovski, C.; Tilley, L. Food Vacuole-Associated Lipid Bodies and Heterogeneous Lipid Environments in the Malaria Parasite Plasmodium falciparum Mol. Microbiol. 2004, 54, 109-122
    • (2004) Mol. Microbiol. , vol.54 , pp. 109-122
    • Jackson, K.E.1    Klonis, N.2    Ferguson, D.J.3    Adisa, A.4    Dogovski, C.5    Tilley, L.6
  • 19
    • 0030045312 scopus 로고    scopus 로고
    • Plasmodium Hemozoin Formation Mediated by Histidine-Rich Proteins
    • Sullivan, D. J., Jr.; Gluzman, I. Y.; Goldberg, D. E. Plasmodium Hemozoin Formation Mediated by Histidine-Rich Proteins Science 1998, 271, 219-222
    • (1998) Science , vol.271 , pp. 219-222
    • Sullivan Jr., D.J.1    Gluzman, I.Y.2    Goldberg, D.E.3
  • 21
    • 0032942185 scopus 로고    scopus 로고
    • Involvement of Lipids in Ferriprotoporphyrin IX Polymerization in Malaria
    • Fitch, C. D.; Cai, G. Z.; Chen, Y. F.; Shoemaker, J. D. Involvement of Lipids in Ferriprotoporphyrin IX Polymerization in Malaria Biochim. Biophys. Acta 1999, 1454, 31-37
    • (1999) Biochim. Biophys. Acta , vol.1454 , pp. 31-37
    • Fitch, C.D.1    Cai, G.Z.2    Chen, Y.F.3    Shoemaker, J.D.4
  • 22
    • 0033827908 scopus 로고    scopus 로고
    • Digestive Vacuolar pH of Intact Intraerythrocytic P. falciparum Either Sensitive or Resistant to Chloroquine
    • Dzekunov, S. M.; Ursos, L. M.; Roepe, P. D. Digestive Vacuolar pH of Intact Intraerythrocytic P. falciparum Either Sensitive or Resistant to Chloroquine Mol. Biochem. Parasitol. 2000, 110, 107-124
    • (2000) Mol. Biochem. Parasitol. , vol.110 , pp. 107-124
    • Dzekunov, S.M.1    Ursos, L.M.2    Roepe, P.D.3
  • 24
    • 0000072220 scopus 로고
    • Studies on Malarial Parasites: IX. Chemical and Metabolic Changes during Growth and Multiplication in Vivo and in Vitro
    • Ball, E. G.; McKee, R. W.; Anfinsen, C. B.; Cruz, W. O.; Geiman, Q. M. Studies on Malarial Parasites: IX. Chemical and Metabolic Changes during Growth and Multiplication in Vivo and in Vitro J. Biol. Chem. 1948, 175, 547-571
    • (1948) J. Biol. Chem. , vol.175 , pp. 547-571
    • Ball, E.G.1    McKee, R.W.2    Anfinsen, C.B.3    Cruz, W.O.4    Geiman, Q.M.5
  • 25
    • 79953855847 scopus 로고    scopus 로고
    • X-ray Microanalysis Investigation of the Changes in Na, K, and Hemoglobin Concentration in Plasmodium falciparum -Infected Red Blood Cells
    • Mauritz, J. M. A.; Seear, R.; Esposito, A.; Kaminski, C. F.; Skepper, J. N.; Warley, A.; Lew, V. L.; Tiffert, T. X-ray Microanalysis Investigation of the Changes in Na, K, and Hemoglobin Concentration in Plasmodium falciparum -Infected Red Blood Cells Biophys. J. 2011, 100, 1438-1445
    • (2011) Biophys. J. , vol.100 , pp. 1438-1445
    • Mauritz, J.M.A.1    Seear, R.2    Esposito, A.3    Kaminski, C.F.4    Skepper, J.N.5    Warley, A.6    Lew, V.L.7    Tiffert, T.8
  • 26
    • 33750088680 scopus 로고    scopus 로고
    • Spinning Disc Confocal Microscopy of Live, Intraerythrocytic Malarial Parasites. 1. Quantification of Hemozoin Development for Drug Sensitive versus Resistant Malaria
    • Gligorijevic, B.; McAllister, R.; Urbach, J. S.; Roepe, P. D. Spinning Disc Confocal Microscopy of Live, Intraerythrocytic Malarial Parasites. 1. Quantification of Hemozoin Development for Drug Sensitive versus Resistant Malaria Biochemistry 2006, 45, 12400-12410
    • (2006) Biochemistry , vol.45 , pp. 12400-12410
    • Gligorijevic, B.1    McAllister, R.2    Urbach, J.S.3    Roepe, P.D.4
  • 28
    • 0036152532 scopus 로고    scopus 로고
    • Intraerythrocytic Plasmodium falciparum Utilizes only a Fraction of the Amino Acids Derived from the Digestion of Host Cell Cytosol for the Biosynthesis of Its Proteins
    • Krugliak, M.; Zhang, J.; Ginsburg, H. Intraerythrocytic Plasmodium falciparum Utilizes Only a Fraction of the Amino Acids Derived from the Digestion of Host Cell Cytosol for the Biosynthesis of Its Proteins Mol. Biochem. Parasitol. 2002, 119, 249-256
    • (2002) Mol. Biochem. Parasitol. , vol.119 , pp. 249-256
    • Krugliak, M.1    Zhang, J.2    Ginsburg, H.3
  • 30
    • 0036720312 scopus 로고    scopus 로고
    • Chloroquine Resistance in the Malarial Parasite Plasmodium falciparum
    • Ursos, L. M. B.; Roepe, P. D. Chloroquine Resistance in the Malarial Parasite Plasmodium falciparum Med. Res. Rev. 2002, 22, 465-491
    • (2002) Med. Res. Rev. , vol.22 , pp. 465-491
    • Ursos, L.M.B.1    Roepe, P.D.2
  • 33
    • 0024440266 scopus 로고
    • Ultrastructure of Plasmodium falciparum "in Vitro". I. Baseline for Drug Effects Evaluation
    • Olliaro, P.; Castelli, P.; Milano, F.; Filice, G.; Carosi, G. Ultrastructure of Plasmodium falciparum "in Vitro". I. Baseline for Drug Effects Evaluation Microbiologica 1989, 12, 7-14
    • (1989) Microbiologica , vol.12 , pp. 7-14
    • Olliaro, P.1    Castelli, P.2    Milano, F.3    Filice, G.4    Carosi, G.5
  • 34
    • 76649123110 scopus 로고    scopus 로고
    • Digestive-Vacuole Genesis and Endocytic Processes in the Early Intraerythrocytic Stages of Plasmodium falciparum
    • Bakar, N. A.; Klonis, N.; Hanssen, E.; Chan, C.; Tilley, L. Digestive-Vacuole Genesis and Endocytic Processes in the Early Intraerythrocytic Stages of Plasmodium falciparum J. Cell Sci. 2009, 123, 441-450
    • (2009) J. Cell Sci. , vol.123 , pp. 441-450
    • Bakar, N.A.1    Klonis, N.2    Hanssen, E.3    Chan, C.4    Tilley, L.5
  • 35
    • 0030596205 scopus 로고    scopus 로고
    • Characterization of Native Falcipain, an Anzyme Involved in Plasmodium falciparum Hemoglobin Degradation
    • Francis, S. E.; Gluzman, I. Y.; Oksman, A.; Banerjee, D.; Goldberg, D. E. Characterization of Native Falcipain, an Anzyme Involved in Plasmodium falciparum Hemoglobin Degradation Mol. Biochem. Parasitol. 1996, 83, 189-200
    • (1996) Mol. Biochem. Parasitol. , vol.83 , pp. 189-200
    • Francis, S.E.1    Gluzman, I.Y.2    Oksman, A.3    Banerjee, D.4    Goldberg, D.E.5
  • 37
    • 0025255254 scopus 로고
    • Hemoglobin Degradation in the Malaria Parasite Plasmodium falciparum: An Ordered Process in a Unique Organelle
    • Goldberg, D. E.; Slater, A. F. G.; Cerami, A.; Henderson, G. B. Hemoglobin Degradation in the Malaria Parasite Plasmodium falciparum: An Ordered Process in a Unique Organelle Proc. Natl. Acad. Sci. U.S.A. 1990, 87, 2931-2935
    • (1990) Proc. Natl. Acad. Sci. U.S.A. , vol.87 , pp. 2931-2935
    • Goldberg, D.E.1    Slater, A.F.G.2    Cerami, A.3    Henderson, G.B.4
  • 38
    • 0025754304 scopus 로고
    • Hemoglobin Degradation in the Human Malaria Pathogen Plasmodium falciparum: A Catabolic Pathway Initiated by a Specific Aspartic Protease
    • Goldberg, D. E.; Slater, A. F. G.; Beavis, R.; Chait, B.; Cerami, A.; Henderson, G. B. Hemoglobin Degradation in the Human Malaria Pathogen Plasmodium falciparum: A Catabolic Pathway Initiated by a Specific Aspartic Protease J. Exp. Med. 1991, 173, 961-969
    • (1991) J. Exp. Med. , vol.173 , pp. 961-969
    • Goldberg, D.E.1    Slater, A.F.G.2    Beavis, R.3    Chait, B.4    Cerami, A.5    Henderson, G.B.6
  • 40
    • 0026695211 scopus 로고
    • The Pathway of Hemoglobin Degradation in Malaria Parasites
    • Goldberg, D. E.; Slater, A. F. The Pathway of Hemoglobin Degradation in Malaria Parasites Parasitol. Today 1992, 8, 280-283
    • (1992) Parasitol. Today , vol.8 , pp. 280-283
    • Goldberg, D.E.1    Slater, A.F.2
  • 41
    • 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
  • 42
    • 0034666133 scopus 로고    scopus 로고
    • Characterization of Native and Recombinant Falcipain-2, a Principal Trophozoite Cysteine Protease and Essential Hemoglobinase of Plasmodium falciparum
    • Shenai, B. R.; Sijwali, P. S.; Singh, A.; Rosenthal, P. J. Characterization of Native and Recombinant Falcipain-2, a Principal Trophozoite Cysteine Protease and Essential Hemoglobinase of Plasmodium falciparum J. Biol. Chem. 2000, 275, 29000-29010
    • (2000) J. Biol. Chem. , vol.275 , pp. 29000-29010
    • Shenai, B.R.1    Sijwali, P.S.2    Singh, A.3    Rosenthal, P.J.4
  • 43
    • 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
  • 44
    • 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
  • 45
    • 0037181136 scopus 로고    scopus 로고
    • Activity and Inhibition of Plasmepsin IV, a New Aspartic Proteinase from the Malaria Parasite, Plasmodium falciparum
    • Wyatt, D. M.; Berry, C. Activity and Inhibition of Plasmepsin IV, a New Aspartic Proteinase from the Malaria Parasite, Plasmodium falciparum FEBS Lett. 2002, 513, 159-162
    • (2002) FEBS Lett. , vol.513 , pp. 159-162
    • Wyatt, D.M.1    Berry, C.2
  • 46
    • 0033527572 scopus 로고    scopus 로고
    • Identification and Characterization of Falcilysin, a Metallopeptidase Involved in Hemoglobin Catabolism within the Malaria Parasite Plasmodium falciparum
    • Eggleson, K. K.; Duffin, K. L.; Goldberg, D. E. Identification and Characterization of Falcilysin, a Metallopeptidase Involved in Hemoglobin Catabolism within the Malaria Parasite Plasmodium falciparum J. Biol. Chem. 1999, 274, 32411-32417
    • (1999) J. Biol. Chem. , vol.274 , pp. 32411-32417
    • Eggleson, K.K.1    Duffin, K.L.2    Goldberg, D.E.3
  • 47
    • 5644247394 scopus 로고    scopus 로고
    • A Plasmodium falciparum Dipeptidyl Aminopeptidase i Participates in Vacuolar Hemoglobin Degradation
    • Klemba, M.; Gluzman, I.; Goldberg, D. E. A Plasmodium falciparum Dipeptidyl Aminopeptidase I Participates in Vacuolar Hemoglobin Degradation J. Biol. Chem. 2004, 279, 43000-43007
    • (2004) J. Biol. Chem. , vol.279 , pp. 43000-43007
    • Klemba, M.1    Gluzman, I.2    Goldberg, D.E.3
  • 48
    • 0030873366 scopus 로고    scopus 로고
    • Generation of Hemoglobin Peptides in the Acidic Digestive Vacuole of Plasmodium falciparum Implicates Peptide Transport in Amino Acid Production
    • Kolakovich, K. A.; Gluzman, I. Y.; Duffin, K. L.; Goldberg, D. E. Generation of Hemoglobin Peptides in the Acidic Digestive Vacuole of Plasmodium falciparum Implicates Peptide Transport in Amino Acid Production Mol. Biochem. Parasitol. 1997, 87, 123-135
    • (1997) Mol. Biochem. Parasitol. , vol.87 , pp. 123-135
    • Kolakovich, K.A.1    Gluzman, I.Y.2    Duffin, K.L.3    Goldberg, D.E.4
  • 49
    • 0034844897 scopus 로고    scopus 로고
    • The Role of Aminopeptidases in Haemoglobin Degradation in Plasmodium falciparum -Infected Erythrocytes
    • Gavigan, C. S.; Dalton, J. P.; Bell, A. The Role of Aminopeptidases in Haemoglobin Degradation in Plasmodium falciparum -Infected Erythrocytes Mol. Biochem. Parasitol. 2001, 117, 37-48
    • (2001) Mol. Biochem. Parasitol. , vol.117 , pp. 37-48
    • Gavigan, C.S.1    Dalton, J.P.2    Bell, A.3
  • 50
    • 37249008065 scopus 로고    scopus 로고
    • Roles for Two Aminopeptidases in Vacuolar Hemoglobin Catabolism in Plasmodium falciparum
    • Dalal, S.; Klemba, M. Roles for Two Aminopeptidases in Vacuolar Hemoglobin Catabolism in Plasmodium falciparum J. Biol. Chem. 2007, 282, 35978-35987
    • (2007) J. Biol. Chem. , vol.282 , pp. 35978-35987
    • Dalal, S.1    Klemba, M.2
  • 51
    • 0036062411 scopus 로고    scopus 로고
    • Properties, Stage-Dependent Expression and Localization of Plasmodium falciparum M1 Family Zinc-Aminopeptidase
    • Allary, M.; Schrevel, J.; Florent, I. Properties, Stage-Dependent Expression and Localization of Plasmodium falciparum M1 Family Zinc-Aminopeptidase Parasitology 2002, 125, 1-10
    • (2002) Parasitology , vol.125 , pp. 1-10
    • Allary, M.1    Schrevel, J.2    Florent, I.3
  • 52
    • 0032583101 scopus 로고    scopus 로고
    • A Plasmodium falciparum Aminopeptidase Gene Belonging to the M1 Family of Zinc-Metallopeptidases Is Expressed in Erythrocytic Stages
    • Florent, I.; Derhy, Z.; Allary, M.; Monsigny, M.; Mayer, R.; Schrével, J. A Plasmodium falciparum Aminopeptidase Gene Belonging to the M1 Family of Zinc-Metallopeptidases Is Expressed in Erythrocytic Stages Mol. Biochem. Parasitol. 1998, 97, 149-160
    • (1998) Mol. Biochem. Parasitol. , vol.97 , pp. 149-160
    • Florent, I.1    Derhy, Z.2    Allary, M.3    Monsigny, M.4    Mayer, R.5    Schrével, J.6
  • 54
    • 0038115341 scopus 로고    scopus 로고
    • The Most Potent Organophosphorus Inhibitors of Leucine Aminopeptidase. Structure-Based Design, Chemistry, and Activity
    • Grembecka, J.; Mucha, A.; Cierpicki, T.; Kafarski, P. The Most Potent Organophosphorus Inhibitors of Leucine Aminopeptidase. Structure-Based Design, Chemistry, and Activity J. Med. Chem. 2003, 46, 2641-2655
    • (2003) J. Med. Chem. , vol.46 , pp. 2641-2655
    • Grembecka, J.1    Mucha, A.2    Cierpicki, T.3    Kafarski, P.4
  • 55
    • 78651379485 scopus 로고    scopus 로고
    • PfCRT-Mediated Drug Transport in Malarial Parasites
    • Roepe, P. D. PfCRT-Mediated Drug Transport in Malarial Parasites Biochemistry 2011, 50, 163-171
    • (2011) Biochemistry , vol.50 , pp. 163-171
    • Roepe, P.D.1
  • 57
    • 33750090345 scopus 로고    scopus 로고
    • Spinning Disk Confocal Microscopy of Live, Intraerythrocytic Malarial Parasites. 2. Altered Vacuolar Volume Regulation in Drug Resistant Malaria
    • Gligorijevic, B.; Bennett, T.; McAllister, R.; Urbach, J. S.; Roepe, P. D. Spinning Disk Confocal Microscopy of Live, Intraerythrocytic Malarial Parasites. 2. Altered Vacuolar Volume Regulation in Drug Resistant Malaria Biochemistry 2006, 45, 12411-12423
    • (2006) Biochemistry , vol.45 , pp. 12411-12423
    • Gligorijevic, B.1    Bennett, T.2    McAllister, R.3    Urbach, J.S.4    Roepe, P.D.5
  • 58
    • 3142618432 scopus 로고    scopus 로고
    • The Antimalarial Drug Resistance Protein Plasmodium falciparum Chloroquine Resistance Transporter Binds Chloroquine
    • Zhang, H.; Paguio, M.; Roepe, P. D. The Antimalarial Drug Resistance Protein Plasmodium falciparum Chloroquine Resistance Transporter Binds Chloroquine Biochemistry 2004, 43, 8290-8296
    • (2004) Biochemistry , vol.43 , pp. 8290-8296
    • Zhang, H.1    Paguio, M.2    Roepe, P.D.3
  • 59
    • 70349524663 scopus 로고    scopus 로고
    • Chloroquine Transport via the Malaria Parasite's Chloroquine Resistance Transporter
    • Martin, R. E.; Marchetti, R. V.; Cowan, A. I.; Howitt, S. M.; Bröer, S.; Kirk, K. Chloroquine Transport via the Malaria Parasite's Chloroquine Resistance Transporter Science 2009, 325, 1680-1682
    • (2009) Science , vol.325 , pp. 1680-1682
    • Martin, R.E.1    Marchetti, R.V.2    Cowan, A.I.3    Howitt, S.M.4    Bröer, S.5    Kirk, K.6
  • 63
    • 0019995366 scopus 로고
    • Mechanism of Autooxidation for Hemoglobins and Myoglobins. Promotion of Superoxide Production by Protons and Anions
    • Wallace, W. J.; Houtchens, R. A.; Maxwell, J. C.; Caughey, W. S. Mechanism of Autooxidation for Hemoglobins and Myoglobins. Promotion of Superoxide Production by Protons and Anions J. Biol. Chem. 1982, 257, 4966-4977
    • (1982) J. Biol. Chem. , vol.257 , pp. 4966-4977
    • Wallace, W.J.1    Houtchens, R.A.2    Maxwell, J.C.3    Caughey, W.S.4
  • 64
    • 0031552067 scopus 로고    scopus 로고
    • Biphasic Nature in the Autoxidation Reaction of Human Oxyhemoglobin
    • Tsuruga, M.; Shikama, K. Biphasic Nature in the Autoxidation Reaction of Human Oxyhemoglobin Biochim. Biophys. Acta 1997, 1337, 86-104
    • (1997) Biochim. Biophys. Acta , vol.1337 , pp. 86-104
    • Tsuruga, M.1    Shikama, K.2
  • 65
    • 0022389401 scopus 로고
    • Low-Temperature Formation of a Distal Histidine Complex in Hemoglobin: A Probe for Heme Pocket Flexibility
    • Levy, A.; Rifkind, J. M. Low-Temperature Formation of a Distal Histidine Complex in Hemoglobin: A Probe for Heme Pocket Flexibility Biochemistry 1985, 24, 6050-6054
    • (1985) Biochemistry , vol.24 , pp. 6050-6054
    • Levy, A.1    Rifkind, J.M.2
  • 66
    • 34147191082 scopus 로고
    • The Reduction of Methemoglobin in Erythrocytes of a Patient with Congenital Methemoglobinemia, Subjects with Erythrocyte Glucose-6-Phosphate Dehydrogenase Deficiency, and Normal Individuals
    • Jaffee, E. R. The Reduction of Methemoglobin in Erythrocytes of a Patient with Congenital Methemoglobinemia, Subjects with Erythrocyte Glucose-6-Phosphate Dehydrogenase Deficiency, and Normal Individuals Blood 1963, 21, 561-572
    • (1963) Blood , vol.21 , pp. 561-572
    • Jaffee, E.R.1
  • 67
    • 84858768957 scopus 로고    scopus 로고
    • Redox Regulation in Malaria: Current Concepts and Pharmacotherapeutic Implications
    • Goyal, M.; Alam, A.; Bandyopadhyay, U. Redox Regulation in Malaria: Current Concepts and Pharmacotherapeutic Implications Curr. Med. Chem. 2012, 19, 1475-1503
    • (2012) Curr. Med. Chem. , vol.19 , pp. 1475-1503
    • Goyal, M.1    Alam, A.2    Bandyopadhyay, U.3
  • 68
    • 0023201135 scopus 로고
    • Comparison of Proteases from Chloroquine-Sensitive and Chloroquine-Resistant Strains of Plasmodium falciparum
    • Vander Jagt, D. L.; Hunsaker, L. A.; Campos, N. M. Comparison of Proteases from Chloroquine-Sensitive and Chloroquine-Resistant Strains of Plasmodium falciparum Biochem. Pharmacol. 1987, 36, 3285-3291
    • (1987) Biochem. Pharmacol. , vol.36 , pp. 3285-3291
    • Vander Jagt, D.L.1    Hunsaker, L.A.2    Campos, N.M.3
  • 70
    • 0038312099 scopus 로고    scopus 로고
    • The treatment of Plasmodium falciparum -Infected Erythrocytes with Chloroquine Leads to Accumulation of Ferriprotoporphyrin-IX Bound to Particular Parasite Proteins and to the Inhibition of the Parasite's 6-Phosphogluconate Dehydrogenase
    • Famin, O.; Ginsburg, H. The treatment of Plasmodium falciparum -Infected Erythrocytes with Chloroquine Leads to Accumulation of Ferriprotoporphyrin-IX Bound to Particular Parasite Proteins and to the Inhibition of the Parasite's 6-Phosphogluconate Dehydrogenase Parasite 2003, 10, 39-50
    • (2003) Parasite , vol.10 , pp. 39-50
    • Famin, O.1    Ginsburg, H.2
  • 71
    • 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
  • 72
    • 16244365509 scopus 로고    scopus 로고
    • Destabilisation and Subsequent Lysis of Human Erythrocytes Induced by Plasmodium falciparum Haem Products
    • Omodeo-Sale, F.; Motti, A.; Dondorp, A.; White, N. J.; Taramelli, D. Destabilisation and Subsequent Lysis of Human Erythrocytes Induced by Plasmodium falciparum Haem Products Eur. J. Haematol. 2005, 74, 324-332
    • (2005) Eur. J. Haematol. , vol.74 , pp. 324-332
    • Omodeo-Sale, F.1    Motti, A.2    Dondorp, A.3    White, N.J.4    Taramelli, D.5
  • 73
    • 19444386445 scopus 로고    scopus 로고
    • Free Heme Toxicity and Its Detoxification Systems in Human
    • Kumar, S.; Bandyopadhyay, U. Free Heme Toxicity and Its Detoxification Systems in Human Toxicol. Lett. 2005, 157, 175-188
    • (2005) Toxicol. Lett. , vol.157 , pp. 175-188
    • Kumar, S.1    Bandyopadhyay, U.2
  • 75
    • 84868310578 scopus 로고    scopus 로고
    • Direct Tests of Enzymatic Heme Degradation by the Malaria Parasite Plasmodium falciparum
    • Sigala, P. A.; Crowley, J. R.; Hsieh, S.; Henderson, J. P.; Goldberg, D. E. Direct Tests of Enzymatic Heme Degradation by the Malaria Parasite Plasmodium falciparum J. Biol. Chem. 2012, 287, 37793-37807
    • (2012) J. Biol. Chem. , vol.287 , pp. 37793-37807
    • Sigala, P.A.1    Crowley, J.R.2    Hsieh, S.3    Henderson, J.P.4    Goldberg, D.E.5
  • 76
    • 0035089693 scopus 로고    scopus 로고
    • Haemoproteus and Schistosoma Synthesize Heme Polymers Similar to Plasmodium Hemozoin and β-Hematin
    • Chen, M. M.; Shi, L.; Sullivan, D. J., Jr. Haemoproteus and Schistosoma Synthesize Heme Polymers Similar to Plasmodium Hemozoin and β-Hematin Mol. Biochem. Parasitol. 2001, 1, 1-8
    • (2001) Mol. Biochem. Parasitol. , vol.1 , pp. 1-8
    • Chen, M.M.1    Shi, L.2    Sullivan Jr., D.J.3
  • 77
    • 0033593057 scopus 로고    scopus 로고
    • Spectroscopic Characterization of the Heme Binding Sites in Plasmodium falciparum Histidine-Rich Protein 2
    • Choi, C. Y.; Cerda, J. F.; Chu, H. A.; Babcock, G. T.; Marletta, M. A. Spectroscopic Characterization of the Heme Binding Sites in Plasmodium falciparum Histidine-Rich Protein 2 Biochemistry 1999, 38, 16916-16924
    • (1999) Biochemistry , vol.38 , pp. 16916-16924
    • Choi, C.Y.1    Cerda, J.F.2    Chu, H.A.3    Babcock, G.T.4    Marletta, M.A.5
  • 78
    • 0035862696 scopus 로고    scopus 로고
    • Antimalarial Drugs Influence the pH Dependent Solubility of Heme via Apparent Nucleation Phenomena
    • Ursos, L. M.; DuBay, K. F.; Roepe, P. D. Antimalarial Drugs Influence the pH Dependent Solubility of Heme via Apparent Nucleation Phenomena Mol. Biochem. Parasitol. 2001, 112, 11-17
    • (2001) Mol. Biochem. Parasitol. , vol.112 , pp. 11-17
    • Ursos, L.M.1    Dubay, K.F.2    Roepe, P.D.3
  • 81
    • 0030870923 scopus 로고    scopus 로고
    • Thermodynamic Factors Controlling the Interaction of Quinoline Antimalarial Drugs with Ferriprotoporphyrin IX
    • Egan, T. J.; Mavuso, W. W.; Ross, D. C.; Marques, H. M. Thermodynamic Factors Controlling the Interaction of Quinoline Antimalarial Drugs with Ferriprotoporphyrin IX J. Inorg. Biochem. 1997, 68, 137-145
    • (1997) J. Inorg. Biochem. , vol.68 , pp. 137-145
    • Egan, T.J.1    Mavuso, W.W.2    Ross, D.C.3    Marques, H.M.4
  • 82
    • 0344665762 scopus 로고    scopus 로고
    • Effects of Solvent Composition and Ionic Strength on the Interaction of Quinoline Antimalarials with Ferriprotoporphyrin IX
    • Egan, T. J.; Ncokazi, K. K. Effects of Solvent Composition and Ionic Strength on the Interaction of Quinoline Antimalarials with Ferriprotoporphyrin IX J. Inorg. Biochem. 2004, 98, 144-152
    • (2004) J. Inorg. Biochem. , vol.98 , pp. 144-152
    • Egan, T.J.1    Ncokazi, K.K.2
  • 83
    • 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
  • 84
    • 0017229966 scopus 로고
    • The Structure of Haem in Pyridine/Water Mixtures and Its Implication in Studies of Haem Catabolism
    • Brown, S. B.; King, R. F. The Structure of Haem in Pyridine/Water Mixtures and Its Implication in Studies of Haem Catabolism Biochem. J. 1976, 153, 479-483
    • (1976) Biochem. J. , vol.153 , pp. 479-483
    • Brown, S.B.1    King, R.F.2
  • 86
    • 84867048396 scopus 로고    scopus 로고
    • Neutral Lipids Associated with Haemozoin Mediate Efficient and Rapid β-Hematin Formation at Physiological pH, Temperature and Ionic Composition
    • Ambele, M. A.; Egan, T. J. Neutral Lipids Associated with Haemozoin Mediate Efficient and Rapid β-Hematin Formation at Physiological pH, Temperature and Ionic Composition Malaria J. 2012, 11, 337
    • (2012) Malaria J. , vol.11 , pp. 337
    • Ambele, M.A.1    Egan, T.J.2
  • 88
    • 79953043258 scopus 로고    scopus 로고
    • Linear Free Energy Relationships Predict Coordination and π-Stacking Interactions of Small Molecules with Ferriprotoporphyrin IX
    • Kuter, D.; Chibale, K.; Egan, T. J. Linear Free Energy Relationships Predict Coordination and π-Stacking Interactions of Small Molecules with Ferriprotoporphyrin IX J. Inorg. Biochem. 2011, 105, 684-692
    • (2011) J. Inorg. Biochem. , vol.105 , pp. 684-692
    • Kuter, D.1    Chibale, K.2    Egan, T.J.3
  • 89
    • 33646474569 scopus 로고    scopus 로고
    • Interactions of Quinoline Antimalarials with Hematin in Solution
    • Egan, T. J. Interactions of Quinoline Antimalarials with Hematin in Solution J. Inorg. Biochem. 2006, 100, 916-926
    • (2006) J. Inorg. Biochem. , vol.100 , pp. 916-926
    • Egan, T.J.1
  • 90
    • 68949155115 scopus 로고    scopus 로고
    • Speciation of Ferriprotoporphyrin IX in Aqueous and Mixed Aqueous Is Controlled by Solvent Identity, pH, and Salt Concentration
    • Asher, C.; de Villiers, K. A.; Egan, T. J. Speciation of Ferriprotoporphyrin IX in Aqueous and Mixed Aqueous Is Controlled by Solvent Identity, pH, and Salt Concentration Inorg. Chem. 2009, 48, 7994-8003
    • (2009) Inorg. Chem. , vol.48 , pp. 7994-8003
    • Asher, C.1    De Villiers, K.A.2    Egan, T.J.3
  • 91
    • 79952987946 scopus 로고    scopus 로고
    • The Hydroxyl Functionality and a Rigid Proximal N Are Required for Forming a Novel Non-Covalent Quinine-Heme Complex
    • Alumasa, J. N.; Gorka, A. P.; Casabianca, L. B.; Comstock, E.; de Dios, A. C.; Roepe, P. D. The Hydroxyl Functionality and a Rigid Proximal N Are Required for Forming a Novel Non-Covalent Quinine-Heme Complex J. Inorg. Biochem. 2011, 105, 467-475
    • (2011) J. Inorg. Biochem. , vol.105 , pp. 467-475
    • Alumasa, J.N.1    Gorka, A.P.2    Casabianca, L.B.3    Comstock, E.4    De Dios, A.C.5    Roepe, P.D.6
  • 92
    • 84872019217 scopus 로고    scopus 로고
    • Relative to Quinine and Quinidine, Their 9-Epimers Exhibit Decreased Cytostatic Activity and Altered Heme Binding but Similar Cytocidal Activity versus Plasmodium falciparum
    • Gorka, A. P.; Sherlach, K. S.; de Dios, A. C.; Roepe, P. D. Relative to Quinine and Quinidine, Their 9-Epimers Exhibit Decreased Cytostatic Activity and Altered Heme Binding but Similar Cytocidal Activity versus Plasmodium falciparum Antimicrob. Agents Chemother. 2013, 57, 365-374
    • (2013) Antimicrob. Agents Chemother. , vol.57 , pp. 365-374
    • Gorka, A.P.1    Sherlach, K.S.2    De Dios, A.C.3    Roepe, P.D.4
  • 94
    • 0042206037 scopus 로고
    • The Determination of the Paramagnetic Susceptibility of Substances in Solution by Nuclear Magnetic Resonance
    • Evans, D. F. The Determination of the Paramagnetic Susceptibility of Substances in Solution by Nuclear Magnetic Resonance J. Chem. Soc. 1959, 2003-2005
    • (1959) J. Chem. Soc. , pp. 2003-2005
    • Evans, D.F.1
  • 95
    • 0037072289 scopus 로고    scopus 로고
    • Solution Structures of Antimalarial Drug-Heme Complexes
    • Leed, A.; DuBay, K.; Sears, D.; de Dios, A. C.; Roepe, P. D. Solution Structures of Antimalarial Drug-Heme Complexes Biochemistry 2002, 41, 10245-10255
    • (2002) Biochemistry , vol.41 , pp. 10245-10255
    • Leed, A.1    Dubay, K.2    Sears, D.3    De Dios, A.C.4    Roepe, P.D.5
  • 96
    • 0000884823 scopus 로고
    • Complex Formation between Chloroquine and Ferrihaemic Acid in Vitro, and Its Effect on the Antimalarial Action of Chloroquine
    • Cohen, S. N.; Phifer, K. O.; Yielding, K. L. Complex Formation between Chloroquine and Ferrihaemic Acid in Vitro, and Its Effect on the Antimalarial Action of Chloroquine Nature 1964, 202, 805-806
    • (1964) Nature , vol.202 , pp. 805-806
    • Cohen, S.N.1    Phifer, K.O.2    Yielding, K.L.3
  • 97
    • 33847631234 scopus 로고    scopus 로고
    • Crystal Nucleation, Growth, and Morphology of the Synthetic Malaria Pigment β-Hematin and the Effect Thereon by Quinoline Additives: The Malaria Pigment as a Target of Various Antimalarial Drugs
    • Solomonov, I.; Osipova, M.; Feldman, Y.; Baehtz, C.; Kjaer, K.; Robinson, I. K.; Webster, G. T.; McNaughton, D.; Wood, B. R.; Weissbuch, I.; Leiserowitz, L. Crystal Nucleation, Growth, and Morphology of the Synthetic Malaria Pigment β-Hematin and the Effect Thereon by Quinoline Additives: The Malaria Pigment as a Target of Various Antimalarial Drugs J. Am. Chem. Soc. 2007, 129, 2615-2627
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 2615-2627
    • Solomonov, I.1    Osipova, M.2    Feldman, Y.3    Baehtz, C.4    Kjaer, K.5    Robinson, I.K.6    Webster, G.T.7    McNaughton, D.8    Wood, B.R.9    Weissbuch, I.10    Leiserowitz, L.11
  • 98
    • 34247563409 scopus 로고    scopus 로고
    • Activity of Piperaquine and Other 4-Aminoquinoline Antiplasmodial Drugs against Chloroquine-Sensitive and Resistant Blood-Stages of Plasmodium falciparum. Role of β-Hematin Inhibition and Drug Concentration in Vacuolar Water- and Lipid-Phases
    • Warhurst, D. C.; Craig, J. C.; Adagu, I. S.; Guy, R. K.; Madrid, P. B.; Fivelman, Q. L. Activity of Piperaquine and Other 4-Aminoquinoline Antiplasmodial Drugs against Chloroquine-Sensitive and Resistant Blood-Stages of Plasmodium falciparum. Role of β-Hematin Inhibition and Drug Concentration in Vacuolar Water- and Lipid-Phases Biochem. Pharmacol. 2007, 73, 1910-1926
    • (2007) Biochem. Pharmacol. , vol.73 , pp. 1910-1926
    • Warhurst, D.C.1    Craig, J.C.2    Adagu, I.S.3    Guy, R.K.4    Madrid, P.B.5    Fivelman, Q.L.6
  • 99
    • 0021885887 scopus 로고
    • A Nuclear Magnetic Resonance Study of the Interactions of Antimalarial Drugs with Porphyrins
    • Moreau, S.; Perly, B.; Chachaty, C.; Deleuze, C. A Nuclear Magnetic Resonance Study of the Interactions of Antimalarial Drugs with Porphyrins Biochim. Biophys. Acta 1985, 840, 107-116
    • (1985) Biochim. Biophys. Acta , vol.840 , pp. 107-116
    • Moreau, S.1    Perly, B.2    Chachaty, C.3    Deleuze, C.4
  • 100
    • 0000161699 scopus 로고
    • UV-Visible and Carbon NMR Studies of Chloroquine Binding to Urohemin i Chloride and Uroporphyrin i in Aqueous Solutions
    • Constantinidis, I.; Satterlee, J. D. UV-Visible and Carbon NMR Studies of Chloroquine Binding to Urohemin I Chloride and Uroporphyrin I in Aqueous Solutions J. Am. Chem. Soc. 1988, 110, 4391-4395
    • (1988) J. Am. Chem. Soc. , vol.110 , pp. 4391-4395
    • Constantinidis, I.1    Satterlee, J.D.2
  • 101
    • 0030271872 scopus 로고    scopus 로고
    • The Interaction of the Heme-Octapeptide, N -Acetylmicroperoxidase-8 with Antimalarial Drugs: Solution Studies and Modeling by Molecular Mechanics Methods
    • Marques, H. M.; Voster, K.; Egan, T. J. The Interaction of the Heme-Octapeptide, N -Acetylmicroperoxidase-8 with Antimalarial Drugs: Solution Studies and Modeling by Molecular Mechanics Methods J. Inorg. Biochem. 1996, 64, 7-23
    • (1996) J. Inorg. Biochem. , vol.64 , pp. 7-23
    • Marques, H.M.1    Voster, K.2    Egan, T.J.3
  • 103
    • 0041696955 scopus 로고    scopus 로고
    • NMR Studies of Chloroquine-Ferriprotoporphyrin IX Complex
    • de Dios, A. C.; Tycko, R.; Ursos, L. M. B.; Roepe, P. D. NMR Studies of Chloroquine-Ferriprotoporphyrin IX Complex J. Phys. Chem. A 2003, 107, 5821-5825
    • (2003) J. Phys. Chem. A , vol.107 , pp. 5821-5825
    • De Dios, A.C.1    Tycko, R.2    Ursos, L.M.B.3    Roepe, P.D.4
  • 104
    • 10044257575 scopus 로고    scopus 로고
    • Structure of the Amodiaquine-FPIX μ-Oxo Dimer Solution Complex at Atomic Resolution
    • de Dios, A. C.; Casabianca, L. B.; Kosar, A.; Roepe, P. D. Structure of the Amodiaquine-FPIX μ-Oxo Dimer Solution Complex at Atomic Resolution Inorg. Chem. 2004, 43, 8078-8084
    • (2004) Inorg. Chem. , vol.43 , pp. 8078-8084
    • De Dios, A.C.1    Casabianca, L.B.2    Kosar, A.3    Roepe, P.D.4
  • 105
    • 33746390915 scopus 로고    scopus 로고
    • Relationship between NMR Shielding and Heme Binding Strength for a Series of 7-Substituted Quinolines
    • Casabianca, L. B.; de Dios, A. C. Relationship between NMR Shielding and Heme Binding Strength for a Series of 7-Substituted Quinolines J. Phys. Chem. A 2006, 110, 7787-7792
    • (2006) J. Phys. Chem. A , vol.110 , pp. 7787-7792
    • Casabianca, L.B.1    De Dios, A.C.2
  • 108
    • 0042139505 scopus 로고    scopus 로고
    • Quinoline Binding Site on Malaria Pigment Crystal: A Rational Pathway for Antimalarial Drug Design
    • Buller, R.; Peterson, M. L.; Almarsson, O.; Leiserowitz, L. Quinoline Binding Site on Malaria Pigment Crystal: A Rational Pathway for Antimalarial Drug Design Cryst. Growth Des. 2002, 2, 553-562
    • (2002) Cryst. Growth Des. , vol.2 , pp. 553-562
    • Buller, R.1    Peterson, M.L.2    Almarsson, O.3    Leiserowitz, L.4
  • 109
    • 0038492779 scopus 로고    scopus 로고
    • Receptor-Drug Association Studies in the Inhibition of the Hematin Aggregation Process of Malaria
    • Portela, C.; Afonso, C. M. M.; Pinto, M. M. M.; Ramos, M. J. Receptor-Drug Association Studies in the Inhibition of the Hematin Aggregation Process of Malaria FEBS Lett. 2003, 547, 217-222
    • (2003) FEBS Lett. , vol.547 , pp. 217-222
    • Portela, C.1    Afonso, C.M.M.2    Pinto, M.M.M.3    Ramos, M.J.4
  • 110
    • 67650066496 scopus 로고    scopus 로고
    • Aggregated Enhanced Raman Scattering in Fe(III)PPIX Solutions: The Effects of Concentration and Chloroquine on Excitonic Interactions
    • Webster, G. T.; McNaughton, D.; Wood, B. R. Aggregated Enhanced Raman Scattering in Fe(III)PPIX Solutions: The Effects of Concentration and Chloroquine on Excitonic Interactions J. Phys. Chem. B. 2009, 113, 6910-6916
    • (2009) J. Phys. Chem. B. , vol.113 , pp. 6910-6916
    • Webster, G.T.1    McNaughton, D.2    Wood, B.R.3
  • 111
    • 84872817411 scopus 로고    scopus 로고
    • The Single Crystal X-ray Structure of β-Hematin DMSO Solvate Grown in the Presence of Chloroquine, a β-Hematin Growth-Rate Inhibitor
    • Gildenhuys, J.; le Roex, T.; Egan, T. J.; de Villiers, K. A. The Single Crystal X-ray Structure of β-Hematin DMSO Solvate Grown in the Presence of Chloroquine, a β-Hematin Growth-Rate Inhibitor J. Am. Chem. Soc. 2013, 135, 1037-1047
    • (2013) J. Am. Chem. Soc. , vol.135 , pp. 1037-1047
    • Gildenhuys, J.1    Le Roex, T.2    Egan, T.J.3    De Villiers, K.A.4
  • 112
    • 0042139505 scopus 로고    scopus 로고
    • Quinoline Binding Site on Malaria Pigment Crystal: A Rational Pathway for Antimalaria Drug Design
    • Buller, R.; Peterson, M. L.; Almarsson, O.; Leiserowitz, L. Quinoline Binding Site on Malaria Pigment Crystal: A Rational Pathway for Antimalaria Drug Design Cryst. Growth Des. 2002, 2, 553-562
    • (2002) Cryst. Growth Des. , vol.2 , pp. 553-562
    • Buller, R.1    Peterson, M.L.2    Almarsson, O.3    Leiserowitz, L.4
  • 113
    • 0021473147 scopus 로고
    • High-Affinity Binding of Quinine to Iron(III) Porphyrins: Novel Formation of Alkoxide Complexes from Alcohols and Amines
    • Behere, D. V.; Goff, H. M. High-Affinity Binding of Quinine to Iron(III) Porphyrins: Novel Formation of Alkoxide Complexes from Alcohols and Amines J. Am. Chem. Soc. 1984, 106, 4945-4950
    • (1984) J. Am. Chem. Soc. , vol.106 , pp. 4945-4950
    • Behere, D.V.1    Goff, H.M.2
  • 114
    • 84860197935 scopus 로고    scopus 로고
    • Iron(III) Protoporphyrin IX Complexes of the Antimalarial Cinchona Alkaloids Quinine and Quinidine
    • de Villiers, K. A.; Gildenhuys, J.; le Roex, T. Iron(III) Protoporphyrin IX Complexes of the Antimalarial Cinchona Alkaloids Quinine and Quinidine ACS Chem. Biol. 2012, 7, 666-671
    • (2012) ACS Chem. Biol. , vol.7 , pp. 666-671
    • De Villiers, K.A.1    Gildenhuys, J.2    Le Roex, T.3
  • 115
    • 46949083309 scopus 로고    scopus 로고
    • The Crystal Structure of Halofantrine-Ferriprotoporphyrin IX and the Mechanism of Action of Arylmethanol Antimalarials
    • de Villiers, K. A.; Marques, H. M.; Egan, T. J. The Crystal Structure of Halofantrine-Ferriprotoporphyrin IX and the Mechanism of Action of Arylmethanol Antimalarials J. Inorg. Biochem. 2008, 102, 1660-1667
    • (2008) J. Inorg. Biochem. , vol.102 , pp. 1660-1667
    • De Villiers, K.A.1    Marques, H.M.2    Egan, T.J.3
  • 116
    • 0026769849 scopus 로고
    • Stereochemical Evaluation of the Relative Activities of the Cinchona Alkaloids against Plasmodium falciparum
    • Karle, J. M.; Karle, I. L.; Gerena, L.; Milhous, W. K. Stereochemical Evaluation of the Relative Activities of the Cinchona Alkaloids against Plasmodium falciparum Antimicrob. Agents Chemother. 1992, 36, 1538-1544
    • (1992) Antimicrob. Agents Chemother. , vol.36 , pp. 1538-1544
    • Karle, J.M.1    Karle, I.L.2    Gerena, L.3    Milhous, W.K.4
  • 117
    • 0019188940 scopus 로고
    • Ferriprotoporphyrin IX Fulfills the Criteria for Identification as the Chloroquine Receptor of Malaria Parasites
    • Chou, A. C.; Chevli, R.; Fitch, C. D. Ferriprotoporphyrin IX Fulfills the Criteria for Identification as the Chloroquine Receptor of Malaria Parasites Biochemistry 1980, 19, 1543-1549
    • (1980) Biochemistry , vol.19 , pp. 1543-1549
    • Chou, A.C.1    Chevli, R.2    Fitch, C.D.3
  • 118
    • 0026514177 scopus 로고
    • Inhibition by Chloroquine of a Novel Haem Polymerase Enzyme Activity in Malaria Trophozoites
    • Slater, A. F. G.; Cerami, A. Inhibition by Chloroquine of a Novel Haem Polymerase Enzyme Activity in Malaria Trophozoites Nature 1992, 355, 167-169
    • (1992) Nature , vol.355 , pp. 167-169
    • Slater, A.F.G.1    Cerami, A.2
  • 119
    • 0027998464 scopus 로고
    • Quinoline Antimalarial Drugs Inhibit Spontaneous Formation of β-Hematin (Malaria Pigment)
    • Egan, T. J.; Ross, D. C.; Adams, P. A. Quinoline Antimalarial Drugs Inhibit Spontaneous Formation of β-Hematin (Malaria Pigment) FEBS Lett. 1994, 352, 54-57
    • (1994) FEBS Lett. , vol.352 , pp. 54-57
    • Egan, T.J.1    Ross, D.C.2    Adams, P.A.3
  • 121
    • 0031041064 scopus 로고    scopus 로고
    • Depolymerization of Malarial Hemozoin: A Novel Reaction Initiated by Blood Schizontocidal Antimalarials
    • Pandey, A. V.; Tekwani, B. L. Depolymerization of Malarial Hemozoin: A Novel Reaction Initiated by Blood Schizontocidal Antimalarials FEBS Lett. 1997, 402, 236-240
    • (1997) FEBS Lett. , vol.402 , pp. 236-240
    • Pandey, A.V.1    Tekwani, B.L.2
  • 123
    • 0031916653 scopus 로고    scopus 로고
    • Relationship between Antimalarial Drug Activity, Accumulation, and Inhibition of Heme Polymerization in Plasmodium falciparum in Vitro
    • Hawley, S. R.; Bray, P. G.; Mungthin, M.; Atkinson, J. D.; O'Neill, P. M.; Ward, S. A. Relationship between Antimalarial Drug Activity, Accumulation, and Inhibition of Heme Polymerization in Plasmodium falciparum in Vitro Antimicrob. Agents Chemother. 1998, 42, 682-686
    • (1998) Antimicrob. Agents Chemother. , vol.42 , pp. 682-686
    • Hawley, S.R.1    Bray, P.G.2    Mungthin, M.3    Atkinson, J.D.4    O'Neill, P.M.5    Ward, S.A.6
  • 124
    • 0031753042 scopus 로고    scopus 로고
    • Central Role of Hemoglobin Degradation in Mechanisms of Action of 4-Aminoquinolines, Quinoline Methanols, and Phenanthrene Methanols
    • Mungthin, M.; Bray, P. G.; Ridley, R. G.; Ward, S. A. Central Role of Hemoglobin Degradation in Mechanisms of Action of 4-Aminoquinolines, Quinoline Methanols, and Phenanthrene Methanols Antimicrob. Agents Chemother. 1998, 42, 2973-2977
    • (1998) Antimicrob. Agents Chemother. , vol.42 , pp. 2973-2977
    • Mungthin, M.1    Bray, P.G.2    Ridley, R.G.3    Ward, S.A.4
  • 125
    • 0033525824 scopus 로고    scopus 로고
    • The Fate of Ferriprotoporphyrin IX in Malaria Infected Erythrocytes in Conjunction with the Mode of Action of Antimalarial Drugs
    • Zhang, J.; Krugliak, M.; Ginsburg, H. The Fate of Ferriprotoporphyrin 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
  • 126
    • 0242408771 scopus 로고    scopus 로고
    • Inhibition of Heme Crystal Growth by Antimalarials and Other Compounds: Implications for Drug Discovery
    • Chong, C. R.; Sullivan, D. J., Jr. Inhibition of Heme Crystal Growth by Antimalarials and Other Compounds: Implications for Drug Discovery Biochem. Pharmacol. 2003, 66, 2201-2212
    • (2003) Biochem. Pharmacol. , vol.66 , pp. 2201-2212
    • Chong, C.R.1    Sullivan Jr., D.J.2
  • 127
    • 20444402643 scopus 로고    scopus 로고
    • Quinolines Decrease the Rate of β-Hematin Formation
    • Egan, T. J.; Ncokazi, K. K. Quinolines Decrease the Rate of β-Hematin Formation J. Inorg. Biochem. 2005, 99, 1532-1539
    • (2005) J. Inorg. Biochem. , vol.99 , pp. 1532-1539
    • Egan, T.J.1    Ncokazi, K.K.2
  • 130
    • 0014218407 scopus 로고
    • Morphological Effects of Chloroquine on Plasmodium berghei in Mice
    • Macomber, P. B.; Spintz, H. Morphological Effects of Chloroquine on Plasmodium berghei in Mice Nature 1967, 214, 937-939
    • (1967) Nature , vol.214 , pp. 937-939
    • MacOmber, P.B.1    Spintz, H.2
  • 131
    • 0019845594 scopus 로고
    • The Quinine-Haemin Interaction and Its Relationship to Antimalarial Activity
    • Warhurst, D. C. The Quinine-Haemin Interaction and Its Relationship to Antimalarial Activity Biochem. Pharmacol. 1981, 30, 3323-3327
    • (1981) Biochem. Pharmacol. , vol.30 , pp. 3323-3327
    • Warhurst, D.C.1
  • 133
    • 0023640693 scopus 로고
    • The State of Ferriprotoporphyrin IX in Malaria Pigment
    • Fitch, C. D.; Kanjananggulpan, P. The State of Ferriprotoporphyrin IX in Malaria Pigment J. Biol. Chem. 1987, 262, 15552-15555
    • (1987) J. Biol. Chem. , vol.262 , pp. 15552-15555
    • Fitch, C.D.1    Kanjananggulpan, P.2
  • 134
    • 0023700854 scopus 로고
    • Interaction of Ferriprotoporphyrin IX with the Antimalarials Amodiaquine and Halofantrine
    • Blauer, G. Interaction of Ferriprotoporphyrin IX with the Antimalarials Amodiaquine and Halofantrine Biochem. Int. 1988, 17, 729-734
    • (1988) Biochem. Int. , vol.17 , pp. 729-734
    • Blauer, G.1
  • 135
    • 0027500822 scopus 로고
    • Further Evidence for the Interaction of the Antimalarial Drug Amodiaquine with Ferriprotoporphyrin IX
    • Blauer, G.; Akkawi, M.; Bauminger, E. R. Further Evidence for the Interaction of the Antimalarial Drug Amodiaquine with Ferriprotoporphyrin IX Biochem. Pharmacol. 1993, 46, 1573-1576
    • (1993) Biochem. Pharmacol. , vol.46 , pp. 1573-1576
    • Blauer, G.1    Akkawi, M.2    Bauminger, E.R.3
  • 136
    • 1542745991 scopus 로고    scopus 로고
    • A Common Mechanism for Blockade of Heme Polymerization by Antimalarial Quinolines
    • Sullivan, D. J.; Matile, H.; Ridley, R. G.; Goldberg, D. E. A Common Mechanism for Blockade of Heme Polymerization by Antimalarial Quinolines J. Biol. Chem. 1998, 273, 31103-31107
    • (1998) J. Biol. Chem. , vol.273 , pp. 31103-31107
    • Sullivan, D.J.1    Matile, H.2    Ridley, R.G.3    Goldberg, D.E.4
  • 137
    • 0034610012 scopus 로고    scopus 로고
    • Interaction of Chloroquine and Its Analogues with Heme: An Isothermal Titration Calorimetric Study
    • Bachhawat, K.; Thomas, C. J.; Surolia, N.; Surolia, A. Interaction of Chloroquine and Its Analogues with Heme: An Isothermal Titration Calorimetric Study Biochem. Biophys. Res. Commun. 2000, 276, 1075-1079
    • (2000) Biochem. Biophys. Res. Commun. , vol.276 , pp. 1075-1079
    • Bachhawat, K.1    Thomas, C.J.2    Surolia, N.3    Surolia, A.4
  • 138
    • 0034719487 scopus 로고    scopus 로고
    • Structure-Function Relationships in Aminoquinolines: Effect of Amino and Chloro Groups on Quinoline-Hematin Complex Formation, Inhibition of β-Hematin Formation, and Antiplasmodial Activity
    • Egan, T. J.; Hunter, R.; Kaschula, C. H.; Marques, H. M.; Misplon, A.; Walden, J. Structure-Function Relationships in Aminoquinolines: Effect of Amino and Chloro Groups on Quinoline-Hematin Complex Formation, Inhibition of β-Hematin Formation, and Antiplasmodial Activity J. Med. Chem. 2000, 43, 283-291
    • (2000) J. Med. Chem. , vol.43 , pp. 283-291
    • Egan, T.J.1    Hunter, R.2    Kaschula, C.H.3    Marques, H.M.4    Misplon, A.5    Walden, J.6
  • 139
    • 0034601111 scopus 로고    scopus 로고
    • Characterization of Chloroquine-Hematin μ-Oxo Dimer Binding by Isothermal Titration Calorimetry
    • Vippagunta, S. R.; Dorn, A.; Ridley, R. G.; Vennerstrom, J. L. Characterization of Chloroquine-Hematin μ-Oxo Dimer Binding by Isothermal Titration Calorimetry Biochim. Biophys. Acta 2000, 1475, 133-140
    • (2000) Biochim. Biophys. Acta , vol.1475 , pp. 133-140
    • Vippagunta, S.R.1    Dorn, A.2    Ridley, R.G.3    Vennerstrom, J.L.4
  • 140
    • 0031847499 scopus 로고    scopus 로고
    • A Microtitre-Based Method for Measuring the Haem Polymerization Inhibitory Activity (HPIA) of Antimalarial Drugs
    • Basilico, N.; Pagani, E.; Monti, D.; Olliaro, P.; Taramelli, D. A Microtitre-Based Method for Measuring the Haem Polymerization Inhibitory Activity (HPIA) of Antimalarial Drugs J. Antimicrob. Chemother. 1998, 42, 55-60
    • (1998) J. Antimicrob. Chemother. , vol.42 , pp. 55-60
    • Basilico, N.1    Pagani, E.2    Monti, D.3    Olliaro, P.4    Taramelli, D.5
  • 141
    • 0032520711 scopus 로고    scopus 로고
    • A Comparison and Analysis of Several Ways to Promote Haematin (Haem) Polymerisation and an Assessment of Its Initiation in Vitro
    • Dorn, A.; Vippagunta, S. R.; Matile, H.; Bubendorf, A.; Vennerstrom, J. L.; Ridley, R. G. A Comparison and Analysis of Several Ways To Promote Haematin (Haem) Polymerisation and an Assessment of Its Initiation in Vitro Biochem. Pharmacol. 1998, 55, 737-747
    • (1998) Biochem. Pharmacol. , vol.55 , pp. 737-747
    • Dorn, A.1    Vippagunta, S.R.2    Matile, H.3    Bubendorf, A.4    Vennerstrom, J.L.5    Ridley, R.G.6
  • 142
    • 0033104207 scopus 로고    scopus 로고
    • A Colorimetric Assay for Heme in Biological Samples Using 96-Well Plates
    • Pandey, A. V.; Joshi, S. K.; Tekwani, B. L.; Chauhan, V. S. A Colorimetric Assay for Heme in Biological Samples Using 96-Well Plates Anal. Biochem. 1999, 268, 159-161
    • (1999) Anal. Biochem. , vol.268 , pp. 159-161
    • Pandey, A.V.1    Joshi, S.K.2    Tekwani, B.L.3    Chauhan, V.S.4
  • 144
    • 0034478079 scopus 로고    scopus 로고
    • Standardization of the Physicochemical Parameters to Assess in Vitro the β-Hematin Inhibitory Activity of Antimalarial Drugs
    • Parapini, S.; Basilico, N.; Pasini, E.; Egan, T. J.; Olliaro, P.; Taramelli, D.; Monti, D. Standardization of the Physicochemical Parameters To Assess in Vitro the β-Hematin Inhibitory Activity of Antimalarial Drugs Exp. Parasitol. 2000, 96, 249-256
    • (2000) Exp. Parasitol. , vol.96 , pp. 249-256
    • Parapini, S.1    Basilico, N.2    Pasini, E.3    Egan, T.J.4    Olliaro, P.5    Taramelli, D.6    Monti, D.7
  • 146
    • 0035955435 scopus 로고    scopus 로고
    • In Vitro β-Hematin Formation Assays with Plasma of Mice Infected with Plasmodium yoelii and Other Parasite Preparations: Comparative Inhibition with Quinoline and Endoperoxide Antimalarials
    • Tripathi, A. K.; Gupta, A.; Garg, S. K.; Tekwani, B. L. In Vitro β-Hematin Formation Assays with Plasma of Mice Infected with Plasmodium yoelii and Other Parasite Preparations: Comparative Inhibition with Quinoline and Endoperoxide Antimalarials Life Sci. 2001, 69, 2725-2733
    • (2001) Life Sci. , vol.69 , pp. 2725-2733
    • Tripathi, A.K.1    Gupta, A.2    Garg, S.K.3    Tekwani, B.L.4
  • 147
    • 0035996090 scopus 로고    scopus 로고
    • Two Novel Assays for the Detection of Haemin-Binding Properties of Antimalarials Evaluated with Compounds Isolated from Medicinal Plants
    • Steele, J. C. P.; Phelps, R. J.; Simmonds, M. S. J.; Warhurst, D. C.; Meyer, D. J. Two Novel Assays for the Detection of Haemin-Binding Properties of Antimalarials Evaluated with Compounds Isolated from Medicinal Plants J. Antimicrob. Chemother. 2002, 50, 25-31
    • (2002) J. Antimicrob. Chemother. , vol.50 , pp. 25-31
    • Steele, J.C.P.1    Phelps, R.J.2    Simmonds, M.S.J.3    Warhurst, D.C.4    Meyer, D.J.5
  • 148
    • 0036296019 scopus 로고    scopus 로고
    • A Physicochemical Mechanism of Hemozoin (β-Hematin) Synthesis by Malaria Parasite
    • Tripathi, A. K.; Garg, S. K.; Tekwani, B. L. A Physicochemical Mechanism of Hemozoin (β-Hematin) Synthesis by Malaria Parasite Biochem. Biophys. Res. Commun. 2002, 290, 595-601
    • (2002) Biochem. Biophys. Res. Commun. , vol.290 , pp. 595-601
    • Tripathi, A.K.1    Garg, S.K.2    Tekwani, B.L.3
  • 149
    • 0242408771 scopus 로고    scopus 로고
    • Inhibition of Heme Crystal Growth by Antimalarials and Other Compounds: Implications for Drug Discovery
    • Chong, C. R.; Sullivan, D. J. Inhibition of Heme Crystal Growth by Antimalarials and Other Compounds: Implications for Drug Discovery Biochem. Pharmacol. 2003, 66, 2201-2212
    • (2003) Biochem. Pharmacol. , vol.66 , pp. 2201-2212
    • Chong, C.R.1    Sullivan, D.J.2
  • 150
    • 0346728681 scopus 로고    scopus 로고
    • Spectrophotometric Determination of de Novo Hemozoin/β-Hematin Formation in an in Vitro Assay
    • Tripathi, A. K.; Khan, S. I.; Walker, L. A.; Tekwani, B. L. Spectrophotometric Determination of de Novo Hemozoin/β-Hematin Formation in an in Vitro Assay Anal. Biochem. 2004, 325, 85-91
    • (2004) Anal. Biochem. , vol.325 , pp. 85-91
    • Tripathi, A.K.1    Khan, S.I.2    Walker, L.A.3    Tekwani, B.L.4
  • 151
    • 14644443491 scopus 로고    scopus 로고
    • A Colorimetric High-Throughput β-Hematin Inhibition Screening Assay for Use in the Search for Antimalarial Compounds
    • Ncokazi, K. K.; Egan, T. J. A Colorimetric High-Throughput β-Hematin Inhibition Screening Assay for Use in the Search for Antimalarial Compounds Anal. Biochem. 2005, 338, 306-319
    • (2005) Anal. Biochem. , vol.338 , pp. 306-319
    • Ncokazi, K.K.1    Egan, T.J.2
  • 152
    • 34248174328 scopus 로고    scopus 로고
    • A Non-Radiolabeled Heme-GSH Interaction Test for the Screening of Antimalarial Compounds
    • Garavito, G.; Monje, M.-C.; Maurel, S.; Valentin, A.; Nepveu, F.; Deharo, E. A Non-Radiolabeled Heme-GSH Interaction Test for the Screening of Antimalarial Compounds Exp. Parasitol. 2007, 116, 311-313
    • (2007) Exp. Parasitol. , vol.116 , pp. 311-313
    • Garavito, G.1    Monje, M.-C.2    Maurel, S.3    Valentin, A.4    Nepveu, F.5    Deharo, E.6
  • 153
    • 33745214879 scopus 로고    scopus 로고
    • A Simple and Rapid Colorimetric Method to Measure Hemozoin Crystal Growth in Vitro
    • Huy, N. T.; Uyen, D. T.; Sasai, M.; Trang, D. T.; Shiono, T.; Harada, S.; Kamei, K. A Simple and Rapid Colorimetric Method To Measure Hemozoin Crystal Growth in Vitro Anal. Biochem. 2006, 354, 305-307
    • (2006) Anal. Biochem. , vol.354 , pp. 305-307
    • Huy, N.T.1    Uyen, D.T.2    Sasai, M.3    Trang, D.T.4    Shiono, T.5    Harada, S.6    Kamei, K.7
  • 154
    • 31844457268 scopus 로고    scopus 로고
    • Inhibition Assay of β-Hematin Formation Initiated by Lecithin for Screening New Antimalarial Drugs
    • Trang, D. T.; Huy, N. T.; Uyen, D. T.; Sasai, M.; Shiono, T.; Harada, S.; Kamei, K. Inhibition Assay of β-Hematin Formation Initiated by Lecithin for Screening New Antimalarial Drugs Anal. Biochem. 2006, 349, 292-296
    • (2006) Anal. Biochem. , vol.349 , pp. 292-296
    • Trang, D.T.1    Huy, N.T.2    Uyen, D.T.3    Sasai, M.4    Shiono, T.5    Harada, S.6    Kamei, K.7
  • 155
    • 33845983685 scopus 로고    scopus 로고
    • Simple Colorimetric Inhibition Assay of Heme Crystallization for High-Throughput Screening of Antimalarial Compounds
    • Huy, N. T.; Uyen, D. T.; Maeda, A.; Trang, D. T.; Oida, T.; Harada, S.; Kamei, K. Simple Colorimetric Inhibition Assay of Heme Crystallization for High-Throughput Screening of Antimalarial Compounds Antimicrob. Agents Chemother. 2007, 51, 350-353
    • (2007) Antimicrob. Agents Chemother. , vol.51 , pp. 350-353
    • Huy, N.T.1    Uyen, D.T.2    Maeda, A.3    Trang, D.T.4    Oida, T.5    Harada, S.6    Kamei, K.7
  • 159
  • 160
  • 161
    • 79952986990 scopus 로고    scopus 로고
    • A Perspective on Antimalarial Action: Effects of Weak Bases on Plasmodium falciparum
    • Krogstad, D. J.; Schlesinger, P. H. A Perspective on Antimalarial Action: Effects of Weak Bases on Plasmodium falciparum Biochem. Pharmacol. 1998, 35, 793-798
    • (1998) Biochem. Pharmacol. , vol.35 , pp. 793-798
    • Krogstad, D.J.1    Schlesinger, P.H.2
  • 162
    • 84860438168 scopus 로고    scopus 로고
    • Investigating the Activity of Quinine Analogues versus Chloroquine Resistant Plasmodium falciparum
    • Dinio, T.; Gorka, A. P.; McGinniss, A.; Roepe, P. D.; Morgan, J. B. Investigating the Activity of Quinine Analogues versus Chloroquine Resistant Plasmodium falciparum Bioorg. Med. Chem. 2011, 20, 3292-3297
    • (2011) Bioorg. Med. Chem. , vol.20 , pp. 3292-3297
    • Dinio, T.1    Gorka, A.P.2    McGinniss, A.3    Roepe, P.D.4    Morgan, J.B.5
  • 163
    • 84865171164 scopus 로고    scopus 로고
    • Autophagy in Apicomplexa: A Life Sustaining Death Mechanism?
    • Sinai, A. P.; Roepe, P. D. Autophagy in Apicomplexa: A Life Sustaining Death Mechanism? Trends Parasitol 2012, 28, 358-364
    • (2012) Trends Parasitol , vol.28 , pp. 358-364
    • Sinai, A.P.1    Roepe, P.D.2
  • 164
    • 72749090340 scopus 로고    scopus 로고
    • Reduced Digestive Vacuolar Accumulation of Chloroquine Is Not Linked to Resistance to Chloroquine Toxicity
    • Cabrera, M.; Paguio, M. F.; Xie, C.; Roepe, P. D. Reduced Digestive Vacuolar Accumulation of Chloroquine Is Not Linked to Resistance to Chloroquine Toxicity Biochemistry 2009, 48, 11152-11154
    • (2009) Biochemistry , vol.48 , pp. 11152-11154
    • Cabrera, M.1    Paguio, M.F.2    Xie, C.3    Roepe, P.D.4
  • 165
    • 79957493743 scopus 로고    scopus 로고
    • Plasmodium falciparum Resistance to Cytocidal versus Cytostatic Effects of Chloroquine
    • Paguio, M. F.; Bogle, K. L.; Roepe, P. D. Plasmodium falciparum Resistance to Cytocidal versus Cytostatic Effects of Chloroquine Mol. Biochem. Parasitol. 2011, 178, 1-6
    • (2011) Mol. Biochem. Parasitol. , vol.178 , pp. 1-6
    • Paguio, M.F.1    Bogle, K.L.2    Roepe, P.D.3
  • 166
    • 18244396971 scopus 로고    scopus 로고
    • Alternative Mutations at Position 76 of the Vacuolar Transmembrane Protein PfCRT Are Associated with Chloroquine Resistance and Unique Stereospecific Quinine and Quinidine Responses in Plasmodium falciparum
    • Cooper, R. A.; Ferdig, M. T.; Su, X. Z.; Ursos, L. M.; Mu, J.; Nomura, T.; Fujioka, H.; Fidock, D. A.; Roepe, P. D.; Wellems, T. E. Alternative Mutations at Position 76 of the Vacuolar Transmembrane Protein PfCRT Are Associated with Chloroquine Resistance and Unique Stereospecific Quinine and Quinidine Responses in Plasmodium falciparum Mol. Pharmacol. 2002, 61, 35-42
    • (2002) Mol. Pharmacol. , vol.61 , pp. 35-42
    • Cooper, R.A.1    Ferdig, M.T.2    Su, X.Z.3    Ursos, L.M.4    Mu, J.5    Nomura, T.6    Fujioka, H.7    Fidock, D.A.8    Roepe, P.D.9    Wellems, T.E.10
  • 167
    • 0037020024 scopus 로고    scopus 로고
    • Chloroquine Resistance in Plasmodium falciparum Malaria Parasites Conferred by pfcrt Mutations
    • Sidhu, A. B.; Verdier-Pinard, D.; Fidock, D. A. Chloroquine Resistance in Plasmodium falciparum Malaria Parasites Conferred by pfcrt Mutations Science 2002, 298, 210-213
    • (2002) Science , vol.298 , pp. 210-213
    • Sidhu, A.B.1    Verdier-Pinard, D.2    Fidock, D.A.3
  • 169
    • 23744435838 scopus 로고    scopus 로고
    • Pfmdr1 Mutations Contribute to Quinine Resistance and Enhance Mefloquine and Artemisinin Sensitivity in Plasmodium falciparum
    • Sidhu, A. B.; Valderramos, S. G.; Fidock, D. A. pfmdr1 Mutations Contribute to Quinine Resistance and Enhance Mefloquine and Artemisinin Sensitivity in Plasmodium falciparum Mol. Microbiol. 2005, 57, 913-926
    • (2005) Mol. Microbiol. , vol.57 , pp. 913-926
    • Sidhu, A.B.1    Valderramos, S.G.2    Fidock, D.A.3
  • 170
    • 33845711820 scopus 로고    scopus 로고
    • Mutations in Transmembrane Domains 1, 4, and 9 of the Plasmodium falciparum Chloroquine Resistance Transporter Alter Susceptibility to Chloroquine, Quinine, and Quinidine
    • Cooper, R. A.; Lane, K. D.; Deng, B.; Mu, J.; Patel, J. J.; Wellems, T. E.; Su, X.; Ferdig, M. T. Mutations in Transmembrane Domains 1, 4, and 9 of the Plasmodium falciparum Chloroquine Resistance Transporter Alter Susceptibility to Chloroquine, Quinine, and Quinidine Mol. Microbiol. 2007, 63, 270-282
    • (2007) Mol. Microbiol. , vol.63 , pp. 270-282
    • Cooper, R.A.1    Lane, K.D.2    Deng, B.3    Mu, J.4    Patel, J.J.5    Wellems, T.E.6    Su, X.7    Ferdig, M.T.8
  • 171
    • 34248338277 scopus 로고    scopus 로고
    • Erratum in
    • Erratum in Mol. Microbiol. 2007, 64, 1139-1148.
    • (2007) Mol. Microbiol. , vol.64 , pp. 1139-1148
  • 173
    • 24944535314 scopus 로고    scopus 로고
    • Primaquine Synergizes the Activity of Chloroquine against Chloroquine-Resistant P. falciparum
    • Bray, P. G.; Deed, S.; Fox, E.; Kalkanidis, M.; Mungthin, M.; Deady, L. W.; Tilley, L.. Primaquine Synergizes the Activity of Chloroquine against Chloroquine-Resistant P. falciparum Biochem. Pharmacol. 2005, 70, 1158-1166
    • (2005) Biochem. Pharmacol. , vol.70 , pp. 1158-1166
    • Bray, P.G.1    Deed, S.2    Fox, E.3    Kalkanidis, M.4    Mungthin, M.5    Deady, L.W.6    Tilley, L.7
  • 175
    • 27644471426 scopus 로고    scopus 로고
    • In Vitro Assessment of Methylene Blue on Chloroquine-Sensitive and -Resistant Plasmodium falciparum Strains Reveals Synergistic Action with Artemisinins
    • Akoachere, M.; Buchholz, K.; Fischer, E.; Burhenne, J.; Haefeli, W. E.; Schirmer, R. H.; Becker, K. In Vitro Assessment of Methylene Blue on Chloroquine-Sensitive and -Resistant Plasmodium falciparum Strains Reveals Synergistic Action with Artemisinins Antimicrob. Agents Chemother. 2005, 49, 4592-4597
    • (2005) Antimicrob. Agents Chemother. , vol.49 , pp. 4592-4597
    • Akoachere, M.1    Buchholz, K.2    Fischer, E.3    Burhenne, J.4    Haefeli, W.E.5    Schirmer, R.H.6    Becker, K.7
  • 176
    • 34347207200 scopus 로고    scopus 로고
    • Blood Schizontocidal Activity of Methylene Blue in Combination with Antimalarials against Plasmodium falciparum
    • Garavito, G.; Bertani, S.; Rincon, J.; Maurel, S.; Monje, M. C.; Landau, I.; Valentin, A.; Deharo, E. Blood Schizontocidal Activity of Methylene Blue in Combination with Antimalarials against Plasmodium falciparum Parasite 2007, 14, 135-140
    • (2007) Parasite , vol.14 , pp. 135-140
    • Garavito, G.1    Bertani, S.2    Rincon, J.3    Maurel, S.4    Monje, M.C.5    Landau, I.6    Valentin, A.7    Deharo, E.8
  • 179
    • 0037142379 scopus 로고    scopus 로고
    • Design, Synthesis, and Evaluation of New Chemosensitizers in Multi-Drug-Resistant Plasmodium falciparum
    • Guan, J.; Kyle, D. E.; Gerena, L.; Zhang, Q.; Milhous, W. K.; Lin, A. J. Design, Synthesis, and Evaluation of New Chemosensitizers in Multi-Drug-Resistant Plasmodium falciparum J. Med. Chem. 2002, 45, 2748-2788
    • (2002) J. Med. Chem. , vol.45 , pp. 2748-2788
    • Guan, J.1    Kyle, D.E.2    Gerena, L.3    Zhang, Q.4    Milhous, W.K.5    Lin, A.J.6
  • 181
    • 77956319522 scopus 로고    scopus 로고
    • Synthesis, Structure-Activity Relationship, and Mode-of-Action Studies of Antimalarial Reversed Chloroquine Compounds
    • Burgess, S. J.; Kelly, J. X.; Shomloo, S.; Wittlin, S.; Brun, R.; Liebmann, K.; Peyton, D. H. Synthesis, Structure-Activity Relationship, and Mode-of-Action Studies of Antimalarial Reversed Chloroquine Compounds J. Med. Chem. 2010, 53, 6477-6489
    • (2010) J. Med. Chem. , vol.53 , pp. 6477-6489
    • Burgess, S.J.1    Kelly, J.X.2    Shomloo, S.3    Wittlin, S.4    Brun, R.5    Liebmann, K.6    Peyton, D.H.7


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