메뉴 건너뛰기




Volumn 10, Issue 3, 2010, Pages 200-216

Pantothenate utilization by plasmodium as a target for antimalarial chemotherapy

Author keywords

Biosynthesis; Coenzyme A; Drug target; Malaria; Metabolism; Pantothenate; Plasmodium; Vitamin

Indexed keywords

ANTIMALARIAL AGENT; COENZYME A; PANTOTHENIC ACID;

EID: 77953739933     PISSN: 18715265     EISSN: None     Source Type: Journal    
DOI: 10.2174/187152610791163390     Document Type: Article
Times cited : (34)

References (141)
  • 1
    • 77249123257 scopus 로고    scopus 로고
    • World Health Organization
    • Geneva
    • World Health Organization. World malaria report 2008; Geneva, 2008.
    • (2008) World malaria report 2008
  • 12
    • 0018606732 scopus 로고
    • Quantitative assessment of antimalarial activity in vitro by a semiautomated microdilution technique
    • Desjardins, R.E.; Canfield, C.J.; Haynes, J.D.; Chulay, J.D. Quantitative assessment of antimalarial activity in vitro by a semiautomated microdilution technique. Antimicrob. Agents Chemother., 1979, 16(6), 710-718.
    • (1979) Antimicrob. Agents Chemother. , vol.16 , Issue.6 , pp. 710-718
    • Desjardins, R.E.1    Canfield, C.J.2    Haynes, J.D.3    Chulay, J.D.4
  • 13
    • 2142640849 scopus 로고    scopus 로고
    • Simple and inexpensive fluorescence-based technique for highthroughput antimalarial drug screening
    • Smilkstein, M.; Sriwilaijaroen, N.; Kelly, J.X.; Wilairat, P.; Riscoe, M. Simple and inexpensive fluorescence-based technique for highthroughput antimalarial drug screening. Antimicrob. Agents Chemother., 2004, 48(5), 1803-1806.
    • (2004) Antimicrob. Agents Chemother. , vol.48 , Issue.5 , pp. 1803-1806
    • Smilkstein, M.1    Sriwilaijaroen, N.2    Kelly, J.X.3    Wilairat, P.4    Riscoe, M.5
  • 15
    • 39049153083 scopus 로고    scopus 로고
    • The fight against drugresistant malaria: Novel plasmodial targets and antimalarial drugs
    • Choi, S.R.; Mukherjee, P.; Avery, M.A. The fight against drugresistant malaria: novel plasmodial targets and antimalarial drugs. Curr. Med. Chem., 2008, 15(2), 161-171.
    • (2008) Curr. Med. Chem. , vol.15 , Issue.2 , pp. 161-171
    • Choi, S.R.1    Mukherjee, P.2    Avery, M.A.3
  • 16
    • 11144352633 scopus 로고
    • Further studies on the survival and development in vitro of a malarial parasite
    • Trager, W. Further studies on the survival and development in vitro of a malarial parasite. J. Exp. Med., 1943, 77(5), 411-420.
    • (1943) J. Exp. Med. , vol.77 , Issue.5 , pp. 411-420
    • Trager, W.1
  • 17
    • 2642681905 scopus 로고
    • The relation between panthothenic acid and Plasmodium gallinaceum infections in the chicken and the antimalarial activity of analogues of pantothenic acid
    • Brackett, S.; Waletzky, E.; Baker, M. The relation between panthothenic acid and Plasmodium gallinaceum infections in the chicken and the antimalarial activity of analogues of pantothenic acid. J. Parasitol., 1946, 32(5), 453-462.
    • (1946) J. Parasitol. , vol.32 , Issue.5 , pp. 453-462
    • Brackett, S.1    Waletzky, E.2    Baker, M.3
  • 18
    • 0021909963 scopus 로고
    • Nutritional requirements of Plasmodium falciparum in culture. I. Exogenously supplied dialyzable components necessary for continuous growth
    • Divo, A.A.; Geary, T.G.; Davis, N.L.; Jensen, J.B. Nutritional requirements of Plasmodium falciparum in culture. I. Exogenously supplied dialyzable components necessary for continuous growth. J. Protozool., 1985, 32(1), 59-64.
    • (1985) J. Protozool. , vol.32 , Issue.1 , pp. 59-64
    • Divo, A.A.1    Geary, T.G.2    Davis, N.L.3    Jensen, J.B.4
  • 19
    • 12944286494 scopus 로고    scopus 로고
    • Provitamin B5 (pantothenol) inhibits growth of the intraerythrocytic malaria parasite
    • Saliba, K.J.; Ferru, I.; Kirk, K. Provitamin B5 (pantothenol) inhibits growth of the intraerythrocytic malaria parasite. Antimicrob. Agents Chemother., 2005, 49(2), 632-637.
    • (2005) Antimicrob. Agents Chemother. , vol.49 , Issue.2 , pp. 632-637
    • Saliba, K.J.1    Ferru, I.2    Kirk, K.3
  • 20
    • 30644456408 scopus 로고    scopus 로고
    • Vitamin B1 de novo synthesis in the human malaria parasite Plasmodium falciparum depends on external provision of 4-amino-5-hydroxymethyl-2-methylpyrimidine
    • Wrenger, C.; Eschbach, M.L.; Muller, I.B.; Laun, N.P.; Begley, T.P.; Walter, R.D. Vitamin B1 de novo synthesis in the human malaria parasite Plasmodium falciparum depends on external provision of 4-amino-5-hydroxymethyl-2-methylpyrimidine. Biol. Chem., 2006, 387(1), 41-51.
    • (2006) Biol. Chem. , vol.387 , Issue.1 , pp. 41-51
    • Wrenger, C.1    Eschbach, M.L.2    Muller, I.B.3    Laun, N.P.4    Begley, T.P.5    Walter, R.D.6
  • 21
    • 33847055382 scopus 로고    scopus 로고
    • Vitamin and cofactor biosynthesis pathways in Plasmodium and other apicomplexan parasites
    • Muller, S.; Kappes, B. Vitamin and cofactor biosynthesis pathways in Plasmodium and other apicomplexan parasites. Trends Parasitol., 2007, 23(3), 112-121.
    • (2007) Trends Parasitol. , vol.23 , Issue.3 , pp. 112-121
    • Muller, S.1    Kappes, B.2
  • 22
    • 0032562763 scopus 로고    scopus 로고
    • Transport and metabolism of the essential vitamin pantothenic acid in human erythrocytes infected with the malaria parasite Plasmodium falciparum
    • Saliba, K.J.; Horner, H.A.; Kirk, K. Transport and metabolism of the essential vitamin pantothenic acid in human erythrocytes infected with the malaria parasite Plasmodium falciparum. J. Biol. Chem., 1998, 273(17), 10190-10195.
    • (1998) J. Biol. Chem. , vol.273 , Issue.17 , pp. 10190-10195
    • Saliba, K.J.1    Horner, H.A.2    Kirk, K.3
  • 23
    • 0035947587 scopus 로고    scopus 로고
    • H+-coupled pantothenate transport in the intracellular malaria parasite
    • Saliba, K.J.; Kirk, K. H+-coupled pantothenate transport in the intracellular malaria parasite. J. Biol. Chem., 2001, 276(21), 18115-18121.
    • (2001) J. Biol. Chem. , vol.276 , Issue.21 , pp. 18115-18121
    • Saliba, K.J.1    Kirk, K.2
  • 24
    • 69949148704 scopus 로고    scopus 로고
    • The human malaria parasite Plasmodium falciparum is not dependent on host coenzyme A biosynthesis
    • Spry, C.; Saliba, K.J. The human malaria parasite Plasmodium falciparum is not dependent on host coenzyme A biosynthesis. J. Biol. Chem., 2009, 284(37), 24904-24913.
    • (2009) J. Biol. Chem. , vol.284 , Issue.37 , pp. 24904-24913
    • Spry, C.1    Saliba, K.J.2
  • 25
    • 0025251655 scopus 로고
    • Properties of permeation pathways induced in the human red cell membrane by malaria parasites
    • Cabantchik, Z.I. Properties of permeation pathways induced in the human red cell membrane by malaria parasites. Blood Cells, 1990, 16(2-3), 421-432.
    • (1990) Blood Cells , vol.16 , Issue.2-3 , pp. 421-432
    • Cabantchik, Z.I.1
  • 26
    • 0028034347 scopus 로고
    • Transport pathways in the malaria-infected erythrocyte: Characterization and their use as potential targets for chemotherapy
    • Ginsburg, H. Transport pathways in the malaria-infected erythrocyte: characterization and their use as potential targets for chemotherapy. Biochem. Pharmacol., 1994, 48(10), 1847-1856.
    • (1994) Biochem. Pharmacol. , vol.48 , Issue.10 , pp. 1847-1856
    • Ginsburg, H.1
  • 27
    • 0020630101 scopus 로고
    • New permeability pathways induced in membranes of Plasmodium falciparum infected erythrocytes
    • Ginsburg, H.; Krugliak, M.; Eidelman, O.; Cabantchik, Z.I. New permeability pathways induced in membranes of Plasmodium falciparum infected erythrocytes. Mol. Biochem. Parasitol., 1983, 8(2), 177-190.
    • (1983) Mol. Biochem. Parasitol. , vol.8 , Issue.2 , pp. 177-190
    • Ginsburg, H.1    Krugliak, M.2    Eidelman, O.3    Cabantchik, Z.I.4
  • 28
    • 0021992698 scopus 로고
    • Characterization of permeation pathways appearing in the host membrane of Plasmodium falciparum infected red blood cells
    • Ginsburg, H.; Kutner, S.; Krugliak, M.; Cabantchik, Z.I. Characterization of permeation pathways appearing in the host membrane of Plasmodium falciparum infected red blood cells. Mol. Biochem. Parasitol., 1985, 14(3), 313-322.
    • (1985) Mol. Biochem. Parasitol. , vol.14 , Issue.3 , pp. 313-322
    • Ginsburg, H.1    Kutner, S.2    Krugliak, M.3    Cabantchik, Z.I.4
  • 29
    • 0028136546 scopus 로고
    • Transport of diverse substrates into malaria-infected erythrocytes via a pathway showing functional characteristics of a chloride channel
    • Kirk, K.; Horner, H.A.; Elford, B.C.; Ellory, J.C.; Newbold, C.I. Transport of diverse substrates into malaria-infected erythrocytes via a pathway showing functional characteristics of a chloride channel. J. Biol. Chem., 1994, 269(5), 3339-3347.
    • (1994) J. Biol. Chem. , vol.269 , Issue.5 , pp. 3339-3347
    • Kirk, K.1    Horner, H.A.2    Elford, B.C.3    Ellory, J.C.4    Newbold, C.I.5
  • 30
    • 0027401744 scopus 로고
    • A nutrientpermeable channel on the intraerythrocytic malaria parasite
    • Desai, S.A.; Krogstad, D.J.; McCleskey, E.W. A nutrientpermeable channel on the intraerythrocytic malaria parasite. Nature, 1993, 362(6421), 643-646.
    • (1993) Nature , vol.362 , Issue.6421 , pp. 643-646
    • Desai, S.A.1    Krogstad, D.J.2    McCleskey, E.W.3
  • 31
    • 34548483181 scopus 로고    scopus 로고
    • Feedback inhibition of pantothenate kinase regulates pantothenol uptake by the malaria parasite
    • Lehane, A.M.; Marchetti, R.V.; Spry, C.; van Schalkwyk, D.A.; Teng, R.; Kirk, K.; Saliba, K.J. Feedback inhibition of pantothenate kinase regulates pantothenol uptake by the malaria parasite. J. Biol. Chem., 2007, 282(35), 25395-25405.
    • (2007) J. Biol. Chem. , vol.282 , Issue.35 , pp. 25395-25405
    • Lehane, A.M.1    Marchetti, R.V.2    Spry, C.3    van Schalkwyk, D.A.4    Teng, R.5    Kirk, K.6    Saliba, K.J.7
  • 32
    • 84920223588 scopus 로고
    • Studies on the extracellular cultivation of an intracellular parasite (avian malaria). II. The effects of malate and of coenzyme A concentrates
    • Trager, W. Studies on the extracellular cultivation of an intracellular parasite (avian malaria). II. The effects of malate and of coenzyme A concentrates. J. Exp. Med., 1952, 96(5), 465-476.
    • (1952) J. Exp. Med. , vol.96 , Issue.5 , pp. 465-476
    • Trager, W.1
  • 33
    • 84989998845 scopus 로고
    • Coenzyme A and the malaria parasite Plasmodium lophurae
    • Trager, W. Coenzyme A and the malaria parasite Plasmodium lophurae. J. Protozool., 1954, 1(4), 231-237.
    • (1954) J. Protozool. , vol.1 , Issue.4 , pp. 231-237
    • Trager, W.1
  • 34
    • 0014088874 scopus 로고
    • Pantothenic acid metabolism during avian malaria infection: Pantothenate kinase activity in duck erythrocytes and in Plasmodium lophurae
    • Bennett, T.P.; Trager, W. Pantothenic acid metabolism during avian malaria infection: pantothenate kinase activity in duck erythrocytes and in Plasmodium lophurae. J. Protozool., 1967, 14(2), 214-216.
    • (1967) J. Protozool. , vol.14 , Issue.2 , pp. 214-216
    • Bennett, T.P.1    Trager, W.2
  • 35
    • 0016699218 scopus 로고
    • Coenzyme A requirement of malaria parasites: Enzymes of coenzyme A biosynthesis in normal duck erythrocytes and erythrocytes infected with Plasmodium lophurae
    • Brohn, F.H.; Trager, W. Coenzyme A requirement of malaria parasites: enzymes of coenzyme A biosynthesis in normal duck erythrocytes and erythrocytes infected with Plasmodium lophurae. Proc. Natl. Acad. Sci. U. S. A., 1975, 72(6), 2456-2458.
    • (1975) Proc. Natl. Acad. Sci. U. S. A. , vol.72 , Issue.6 , pp. 2456-2458
    • Brohn, F.H.1    Trager, W.2
  • 36
    • 0035234935 scopus 로고    scopus 로고
    • The biosynthesis of coenzyme A in bacteria
    • Begley, T.P.; Kinsland, C.; Strauss, E. The biosynthesis of coenzyme A in bacteria. Vitam. Horm., 2001, 61, 157-171.
    • (2001) Vitam. Horm. , vol.61 , pp. 157-171
    • Begley, T.P.1    Kinsland, C.2    Strauss, E.3
  • 37
    • 34547102510 scopus 로고    scopus 로고
    • The ubiquitous carrier protein--a window to metabolite biosynthesis
    • Mercer, A.C.; Burkart, M.D. The ubiquitous carrier protein--a window to metabolite biosynthesis. Nat. Prod. Rep., 2007, 24(4), 750-773.
    • (2007) Nat. Prod. Rep. , vol.24 , Issue.4 , pp. 750-773
    • Mercer, A.C.1    Burkart, M.D.2
  • 39
    • 33646933886 scopus 로고    scopus 로고
    • Recombinant expression and biochemical characterization of the unique elongating beta-ketoacyl-acyl carrier protein synthase involved in fatty acid biosynthesis of Plasmodium falciparum using natural and artificial substrates
    • Lack, G.; Homberger-Zizzari, E.; Folkers, G.; Scapozza, L.; Perozzo, R. Recombinant expression and biochemical characterization of the unique elongating beta-ketoacyl-acyl carrier protein synthase involved in fatty acid biosynthesis of Plasmodium falciparum using natural and artificial substrates. J. Biol. Chem., 2006, 281(14), 9538-9546.
    • (2006) J. Biol. Chem. , vol.281 , Issue.14 , pp. 9538-9546
    • Lack, G.1    Homberger-Zizzari, E.2    Folkers, G.3    Scapozza, L.4    Perozzo, R.5
  • 40
    • 0037470835 scopus 로고    scopus 로고
    • Functional characterization of beta-ketoacyl-ACP reductase (FabG) from Plasmodium falciparum
    • Pillai, S.; Rajagopal, C.; Kapoor, M.; Kumar, G.; Gupta, A.; Surolia, N. Functional characterization of beta-ketoacyl-ACP reductase (FabG) from Plasmodium falciparum. Biochem. Biophys. Res. Commun., 2003, 303(1), 387-392.
    • (2003) Biochem. Biophys. Res. Commun. , vol.303 , Issue.1 , pp. 387-392
    • Pillai, S.1    Rajagopal, C.2    Kapoor, M.3    Kumar, G.4    Gupta, A.5    Surolia, N.6
  • 41
    • 0037417775 scopus 로고    scopus 로고
    • The initiating steps of a type II fatty acid synthase in Plasmodium falciparum are catalyzed by pfACP, pfMCAT, and pfKASIII
    • Prigge, S.T.; He, X.; Gerena, L.; Waters, N.C.; Reynolds, K.A. The initiating steps of a type II fatty acid synthase in Plasmodium falciparum are catalyzed by pfACP, pfMCAT, and pfKASIII. Biochemistry, 2003, 42(4), 1160-1169.
    • (2003) Biochemistry , vol.42 , Issue.4 , pp. 1160-1169
    • Prigge, S.T.1    He, X.2    Gerena, L.3    Waters, N.C.4    Reynolds, K.A.5
  • 42
    • 0242580787 scopus 로고    scopus 로고
    • Identification, characterization, and inhibition of Plasmodium falciparum betahydroxyacyl-acyl carrier protein dehydratase (FabZ)
    • Sharma, S.K.; Kapoor, M.; Ramya, T.N.; Kumar, S.; Kumar, G.; Modak, R.; Sharma, S.; Surolia, N.; Surolia, A. Identification, characterization, and inhibition of Plasmodium falciparum betahydroxyacyl-acyl carrier protein dehydratase (FabZ). J. Biol. Chem., 2003, 278(46), 45661-45671.
    • (2003) J. Biol. Chem. , vol.278 , Issue.46 , pp. 45661-45671
    • Sharma, S.K.1    Kapoor, M.2    Ramya, T.N.3    Kumar, S.4    Kumar, G.5    Modak, R.6    Sharma, S.7    Surolia, N.8    Surolia, A.9
  • 43
    • 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(2), 167-173.
    • (2001) Nat. Med. , vol.7 , Issue.2 , pp. 167-173
    • Surolia, N.1    Surolia, A.2
  • 45
    • 33746273843 scopus 로고    scopus 로고
    • Identification and stoichiometry of glycosylphosphatidylinositol-anchored membrane proteins of the human malaria parasite Plasmodium falciparum
    • Gilson, P.R.; Nebl, T.; Vukcevic, D.; Moritz, R.L.; Sargeant, T.; Speed, T.P.; Schofield, L.; Crabb, B.S. Identification and stoichiometry of glycosylphosphatidylinositol-anchored membrane proteins of the human malaria parasite Plasmodium falciparum. Mol. Cell Proteomics, 2006, 5(7), 1286-1299.
    • (2006) Mol. Cell Proteomics , vol.5 , Issue.7 , pp. 1286-1299
    • Gilson, P.R.1    Nebl, T.2    Vukcevic, D.3    Moritz, R.L.4    Sargeant, T.5    Speed, T.P.6    Schofield, L.7    Crabb, B.S.8
  • 46
    • 2342446230 scopus 로고    scopus 로고
    • Developmental-stagespecific triacylglycerol biosynthesis, degradation and trafficking as lipid bodies in Plasmodium falciparum-infected erythrocytes
    • Palacpac, N.M.; Hiramine, Y.; Mi-ichi, F.; Torii, M.; Kita, K.; Hiramatsu, R.; Horii, T.; Mitamura, T. Developmental-stagespecific triacylglycerol biosynthesis, degradation and trafficking as lipid bodies in Plasmodium falciparum-infected erythrocytes. J. Cell Sci., 2004, 117(pt. 8), 1469-1480.
    • (2004) J. Cell Sci. , vol.117 , Issue.pt. 8 , pp. 1469-1480
    • Palacpac, N.M.1    Hiramine, Y.2    Mi-ichi, F.3    Torii, M.4    Kita, K.5    Hiramatsu, R.6    Horii, T.7    Mitamura, T.8
  • 47
    • 0019953147 scopus 로고
    • Phospholipid biosynthesis in synchronous Plasmodium falciparum cultures
    • Vial, H.J.; Thuet, M.J.; Philippot, J.R. Phospholipid biosynthesis in synchronous Plasmodium falciparum cultures. J. Protozool., 1982, 29(2), 258-263.
    • (1982) J. Protozool. , vol.29 , Issue.2 , pp. 258-263
    • Vial, H.J.1    Thuet, M.J.2    Philippot, J.R.3
  • 50
    • 0030885712 scopus 로고    scopus 로고
    • Fatty acid activation
    • Watkins, P.A. Fatty acid activation. Prog. Lipid Res., 1997, 36(1), 55-83.
    • (1997) Prog. Lipid Res. , vol.36 , Issue.1 , pp. 55-83
    • Watkins, P.A.1
  • 52
    • 0344931797 scopus 로고    scopus 로고
    • The cloning and expression of Pfacs1, a Plasmodium falciparum fatty acyl coenzyme A synthetase-1 targeted to the host erythrocyte cytoplasm
    • Matesanz, F.; Duran-Chica, I.; Alcina, A. The cloning and expression of Pfacs1, a Plasmodium falciparum fatty acyl coenzyme A synthetase-1 targeted to the host erythrocyte cytoplasm. J. Mol. Biol., 1999, 291(1), 59-70.
    • (1999) J. Mol. Biol. , vol.291 , Issue.1 , pp. 59-70
    • Matesanz, F.1    Duran-Chica, I.2    Alcina, A.3
  • 53
    • 0037244046 scopus 로고    scopus 로고
    • The Plasmodium falciparum fatty acyl-CoA synthetase family (PfACS) and differential stage-specific expression in infected erythrocytes
    • Matesanz, F.; Tellez, M.M.; Alcina, A. The Plasmodium falciparum fatty acyl-CoA synthetase family (PfACS) and differential stage-specific expression in infected erythrocytes. Mol. Biochem. Parasitol., 2003, 126(1), 109-112.
    • (2003) Mol. Biochem. Parasitol. , vol.126 , Issue.1 , pp. 109-112
    • Matesanz, F.1    Tellez, M.M.2    Alcina, A.3
  • 54
    • 0023875602 scopus 로고
    • Acyl-CoA synthetase activity in Plasmodium knowlesi-infected erythrocytes displays peculiar substrate specificities
    • Beaumelle, B.D.; Vial, H.J. Acyl-CoA synthetase activity in Plasmodium knowlesi-infected erythrocytes displays peculiar substrate specificities. Biochim. Biophys. Acta, 1988, 958(1), 1-9.
    • (1988) Biochim. Biophys. Acta , vol.958 , Issue.1 , pp. 1-9
    • Beaumelle, B.D.1    Vial, H.J.2
  • 55
    • 33750212742 scopus 로고    scopus 로고
    • Intraerythrocytic Plasmodium falciparum utilize a broad range of serum-derived fatty acids with limited modification for their growth
    • Mi-Ichi, F.; Kita, K.; Mitamura, T. Intraerythrocytic Plasmodium falciparum utilize a broad range of serum-derived fatty acids with limited modification for their growth. Parasitology, 2006, 133(pt. 4), 399-410.
    • (2006) Parasitology , vol.133 , Issue.pt. 4 , pp. 399-410
    • Mi-Ichi, F.1    Kita, K.2    Mitamura, T.3
  • 56
    • 0033571612 scopus 로고    scopus 로고
    • Identification and molecular characterization of acyl-CoA synthetase in human erythrocytes and erythroid precursors
    • Malhotra, K.T.; Malhotra, K.; Lubin, B.H.; Kuypers, F.A. Identification and molecular characterization of acyl-CoA synthetase in human erythrocytes and erythroid precursors. Biochem. J., 1999, 344(pt.1), 135-143.
    • (1999) Biochem. J. , vol.344 , Issue.pt.1 , pp. 135-143
    • Malhotra, K.T.1    Malhotra, K.2    Lubin, B.H.3    Kuypers, F.A.4
  • 57
    • 0022347253 scopus 로고
    • Erythrocyte membrane acyl:CoA synthetase activity
    • Davidson, B.C.; Cantrill, R.C. Erythrocyte membrane acyl:CoA synthetase activity. FEBS Lett., 1985, 193(1), 69-74.
    • (1985) FEBS Lett. , vol.193 , Issue.1 , pp. 69-74
    • Davidson, B.C.1    Cantrill, R.C.2
  • 58
    • 4243071596 scopus 로고    scopus 로고
    • The transcriptome of the intraerythrocytic developmental cycle of Plasmodium falciparum
    • Bozdech, Z.; Llinas, M.; Pulliam, B.L.; Wong, E.D.; Zhu, J.; DeRisi, J.L. The transcriptome of the intraerythrocytic developmental cycle of Plasmodium falciparum. PLoS Biol., 2003, 1(1), E5.
    • (2003) PLoS Biol. , vol.1 , Issue.1
    • Bozdech, Z.1    Llinas, M.2    Pulliam, B.L.3    Wong, E.D.4    Zhu, J.5    DeRisi, J.L.6
  • 60
    • 0344908963 scopus 로고
    • The incorporation of radioactivity from [14C]glucose into the soluble metabolic intermediates of malaria parasites
    • Bryant, C.; Voller, A.; Smith, M.J. The incorporation of radioactivity from [14C]glucose into the soluble metabolic intermediates of malaria parasites. Am. J. Trop. Med. Hyg., 1964, 13(4), 515-519.
    • (1964) Am. J. Trop. Med. Hyg. , vol.13 , Issue.4 , pp. 515-519
    • Bryant, C.1    Voller, A.2    Smith, M.J.3
  • 61
    • 0000633508 scopus 로고
    • Carbohydrate metabolism in Plasmodium knowlesi
    • Scheibel, L.W.; Pflaum, W.K. Carbohydrate metabolism in Plasmodium knowlesi. Comp. Biochem. Physiol., 1970, 37(4), 543-553.
    • (1970) Comp. Biochem. Physiol. , vol.37 , Issue.4 , pp. 543-553
    • Scheibel, L.W.1    Pflaum, W.K.2
  • 62
    • 12344312032 scopus 로고    scopus 로고
    • The malaria parasite Plasmodium falciparum has only one pyruvate dehydrogenase complex, which is located in the apicoplast
    • Foth, B.J.; Stimmler, L.M.; Handman, E.; Crabb, B.S.; Hodder, A.N.; McFadden, G.I. The malaria parasite Plasmodium falciparum has only one pyruvate dehydrogenase complex, which is located in the apicoplast. Mol. Microbiol., 2005, 55(1), 39-53.
    • (2005) Mol. Microbiol. , vol.55 , Issue.1 , pp. 39-53
    • Foth, B.J.1    Stimmler, L.M.2    Handman, E.3    Crabb, B.S.4    Hodder, A.N.5    McFadden, G.I.6
  • 63
    • 33744956145 scopus 로고    scopus 로고
    • Metabolic maps and functions of the Plasmodium mitochondrion
    • van Dooren, G.G.; Stimmler, L.M.; McFadden, G.I. Metabolic maps and functions of the Plasmodium mitochondrion. FEMS Microbiol. Rev., 2006, 30(4), 596-630.
    • (2006) FEMS Microbiol. Rev. , vol.30 , Issue.4 , pp. 596-630
    • van Dooren, G.G.1    Stimmler, L.M.2    McFadden, G.I.3
  • 64
    • 64949105863 scopus 로고    scopus 로고
    • Metabolite profiling of the intraerythrocytic malaria parasite Plasmodium falciparum by 1H NMR spectroscopy
    • Teng, R.; Junankar, P.R.; Bubb, W.A.; Rae, C.; Mercier, P.; Kirk, K. Metabolite profiling of the intraerythrocytic malaria parasite Plasmodium falciparum by 1H NMR spectroscopy. NMR Biomed., 2009, 22(3), 292-302.
    • (2009) NMR Biomed. , vol.22 , Issue.3 , pp. 292-302
    • Teng, R.1    Junankar, P.R.2    Bubb, W.A.3    Rae, C.4    Mercier, P.5    Kirk, K.6
  • 65
    • 0016732423 scopus 로고
    • Coezyme A requirement of malaria parasites: Effects of coenzyme A precursors on extracellular development in vitro of Plasmodium lophurae
    • Trager, W.; Brohn, F.H. Coezyme A requirement of malaria parasites: effects of coenzyme A precursors on extracellular development in vitro of Plasmodium lophurae. Proc. Natl. Acad. Sci. USA, 1975, 72(5), 1834-1837.
    • (1975) Proc. Natl. Acad. Sci. USA , vol.72 , Issue.5 , pp. 1834-1837
    • Trager, W.1    Brohn, F.H.2
  • 66
    • 0036596398 scopus 로고    scopus 로고
    • Loose ends: Axenic culture, parasitophorous vacuoles, bird malaria
    • Trager, W. Loose ends: axenic culture, parasitophorous vacuoles, bird malaria. Parassitologia, 2002, 44(1-2), 117-121.
    • (2002) Parassitologia , vol.44 , Issue.1-2 , pp. 117-121
    • Trager, W.1
  • 67
    • 0026650465 scopus 로고
    • Extracellular (axenic) development in vitro of the erythrocytic cycle of Plasmodium falciparum
    • Trager, W.; Williams, J. Extracellular (axenic) development in vitro of the erythrocytic cycle of Plasmodium falciparum. Proc. Natl. Acad. Sci. USA, 1992, 89(12), 5351-5355.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , Issue.12 , pp. 5351-5355
    • Trager, W.1    Williams, J.2
  • 68
    • 0025375451 scopus 로고
    • Initial extracellular development in vitro of erythrocytic stages of malaria parasites (Plasmodium falciparum)
    • Trager, W.; Zung, J.; Tershakovec, M. Initial extracellular development in vitro of erythrocytic stages of malaria parasites (Plasmodium falciparum). Proc. Natl. Acad. Sci. USA, 1990, 87(15), 5618-5622.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , Issue.15 , pp. 5618-5622
    • Trager, W.1    Zung, J.2    Tershakovec, M.3
  • 69
    • 3242754218 scopus 로고    scopus 로고
    • Specific labeling of cell surface proteins with chemically diverse compounds
    • George, N.; Pick, H.; Vogel, H.; Johnsson, N.; Johnsson, K. Specific labeling of cell surface proteins with chemically diverse compounds. J. Am. Chem. Soc., 2004, 126(29), 8896-8897.
    • (2004) J. Am. Chem. Soc. , vol.126 , Issue.29 , pp. 8896-8897
    • George, N.1    Pick, H.2    Vogel, H.3    Johnsson, N.4    Johnsson, K.5
  • 71
    • 23644454829 scopus 로고    scopus 로고
    • Fluorescent multiplex analysis of carrier protein post-translational modification
    • Mercer, A.C.; La Clair, J.J.; Burkart, M.D. Fluorescent multiplex analysis of carrier protein post-translational modification. ChemBioChem, 2005, 6(8), 1335-1337.
    • (2005) ChemBioChem , vol.6 , Issue.8 , pp. 1335-1337
    • Mercer, A.C.1    La Clair, J.J.2    Burkart, M.D.3
  • 72
    • 33846233839 scopus 로고    scopus 로고
    • One-pot preparation of coenzyme A analogues via an improved chemo-enzymatic synthesis of pre-CoA thioester synthons
    • van Wyk, M.; Strauss, E. One-pot preparation of coenzyme A analogues via an improved chemo-enzymatic synthesis of pre-CoA thioester synthons. Chem. Commun. (Camb.), 2007, (4), 398-400.
    • (2007) Chem. Commun. (Camb.) , vol.4 , pp. 398-400
    • van Wyk, M.1    Strauss, E.2
  • 73
    • 33645699855 scopus 로고    scopus 로고
    • One-pot chemo-enzymatic synthesis of reporter-modified proteins
    • Worthington, A.S.; Burkart, M.D. One-pot chemo-enzymatic synthesis of reporter-modified proteins. Org. Biomol. Chem., 2006, 4(1), 44-46.
    • (2006) Org. Biomol. Chem. , vol.4 , Issue.1 , pp. 44-46
    • Worthington, A.S.1    Burkart, M.D.2
  • 74
    • 3042546498 scopus 로고    scopus 로고
    • Labeling proteins with small molecules by site-specific posttranslational modification
    • Yin, J.; Liu, F.; Li, X.H.; Walsh, C.T. Labeling proteins with small molecules by site-specific posttranslational modification. J. Am. Chem. Soc., 2004, 126(25), 7754-7755.
    • (2004) J. Am. Chem. Soc. , vol.126 , Issue.25 , pp. 7754-7755
    • Yin, J.1    Liu, F.2    Li, X.H.3    Walsh, C.T.4
  • 77
    • 12444258931 scopus 로고
    • Chemical series of potential interest
    • In: Wiselogle F.Y., Ed.; J. W. Edwards: Michigan
    • Blanchard, K.C.; Schmid, L.H. Chemical series of potential interest. In: A survey of antimalarial drugs 1941-1945; Wiselogle, F.Y., Ed.; J. W. Edwards: Michigan, 1946; pp. 73-175.
    • (1946) A survey of antimalarial drugs 1941-1945 , pp. 73-175
    • Blanchard, K.C.1    Schmid, L.H.2
  • 78
    • 37349028091 scopus 로고
    • Antagonism of calcium pantothenate for the antimalarial effect of pantoyltaurylamide
    • Cantrell, W. Antagonism of calcium pantothenate for the antimalarial effect of pantoyltaurylamide. J. Parasitol., 1949, 35(2), 219-220.
    • (1949) J. Parasitol. , vol.35 , Issue.2 , pp. 219-220
    • Cantrell, W.1
  • 79
    • 16244405628 scopus 로고    scopus 로고
    • CJ-15,801, a fungal natural product, inhibits the intraerythrocytic stage of Plasmodium falciparum in vitro via an effect on pantothenic acid utilisation
    • Saliba, K.J.; Kirk, K. CJ-15,801, a fungal natural product, inhibits the intraerythrocytic stage of Plasmodium falciparum in vitro via an effect on pantothenic acid utilisation. Mol. Biochem. Parasitol., 2005, 141(1), 129-131.
    • (2005) Mol. Biochem. Parasitol. , vol.141 , Issue.1 , pp. 129-131
    • Saliba, K.J.1    Kirk, K.2
  • 80
    • 37349019498 scopus 로고
    • The synthesis of potential antimalarials - derivatives of α,γ-dihydroxy-β,β-dimethyl-N-ethylbutyramide
    • Senear, A.E.; Rapport, M.M.; Koepfli, J.B. The synthesis of potential antimalarials - derivatives of α,γ-dihydroxy-β,β-dimethyl-N-ethylbutyramide. J. Biol. Chem., 1947, 167(1), 229-234.
    • (1947) J. Biol. Chem. , vol.167 , Issue.1 , pp. 229-234
    • Senear, A.E.1    Rapport, M.M.2    Koepfli, J.B.3
  • 81
    • 27644471425 scopus 로고    scopus 로고
    • A class of pantothenic acid analogs inhibits Plasmodium falciparum pantothenate kinase and represses the proliferation of malaria parasites
    • Spry, C.; Chai, C.L.; Kirk, K.; Saliba, K.J. A class of pantothenic acid analogs inhibits Plasmodium falciparum pantothenate kinase and represses the proliferation of malaria parasites. Antimicrob. Agents Chemother., 2005, 49(11), 4649-4657.
    • (2005) Antimicrob. Agents Chemother. , vol.49 , Issue.11 , pp. 4649-4657
    • Spry, C.1    Chai, C.L.2    Kirk, K.3    Saliba, K.J.4
  • 82
    • 0013914767 scopus 로고
    • Coenzyme A and the antimalarial action in vitro of antipantothenate against Plasmodium lophurae, P. coatneyi and P. falciparum
    • Trager, W. Coenzyme A and the antimalarial action in vitro of antipantothenate against Plasmodium lophurae, P. coatneyi and P. falciparum. Trans. N Y Acad. Sci., 1966, 28(8), 1094-1108.
    • (1966) Trans. N Y Acad. Sci. , vol.28 , Issue.8 , pp. 1094-1108
    • Trager, W.1
  • 84
    • 11144261259 scopus 로고
    • Phenyl pantothenone, an antagonist of pantothenic acid
    • Woolley, D.W.; Collyer, M.L. Phenyl pantothenone, an antagonist of pantothenic acid. J. Biol. Chem., 1945, 159(2), 263-271.
    • (1945) J. Biol. Chem. , vol.159 , Issue.2 , pp. 263-271
    • Woolley, D.W.1    Collyer, M.L.2
  • 85
    • 37349009047 scopus 로고
    • Toxicity and pharmacology of SN-13592 - an analogue of phenyl pantothenone
    • Singher, H.O.; Millman, N.; Bosworth, M.R. Toxicity and pharmacology of SN-13592 - an analogue of phenyl pantothenone. Proc. Soc. Exp. Biol. Med., 1948, 67(3), 388-390.
    • (1948) Proc. Soc. Exp. Biol. Med. , vol.67 , Issue.3 , pp. 388-390
    • Singher, H.O.1    Millman, N.2    Bosworth, M.R.3
  • 86
    • 37349117988 scopus 로고    scopus 로고
    • Coenzyme A biosynthesis: An antimicrobial drug target
    • Spry, C.; Kirk, K.; Saliba, K.J. Coenzyme A biosynthesis: an antimicrobial drug target. FEMS Microbiol. Rev., 2008, 32(1), 56-106.
    • (2008) FEMS Microbiol. Rev. , vol.32 , Issue.1 , pp. 56-106
    • Spry, C.1    Kirk, K.2    Saliba, K.J.3
  • 88
    • 12744253952 scopus 로고    scopus 로고
    • The new permeability pathways: Targets and selective routes for the development of new antimalarial agents
    • Staines, H.M.; Ellory, J.C.; Chibale, K. The new permeability pathways: targets and selective routes for the development of new antimalarial agents. Comb. Chem. High Throughput Screen., 2005, 8(1), 81-88.
    • (2005) Comb. Chem. High Throughput Screen. , vol.8 , Issue.1 , pp. 81-88
    • Staines, H.M.1    Ellory, J.C.2    Chibale, K.3
  • 89
    • 0028834971 scopus 로고
    • In search of a selective inhibitor of the induced transport of small solutes in Plasmodium falciparuminfected erythrocytes: Effects of arylaminobenzoates
    • Kirk, K.; Horner, H.A. In search of a selective inhibitor of the induced transport of small solutes in Plasmodium falciparuminfected erythrocytes: effects of arylaminobenzoates. Biochem. J., 1995, 311(pt. 3), 761-768.
    • (1995) Biochem. J. , vol.311 , Issue.pt. 3 , pp. 761-768
    • Kirk, K.1    Horner, H.A.2
  • 90
    • 0347418183 scopus 로고    scopus 로고
    • Furosemide analogues as potent inhibitors of the new permeability pathways of Plasmodium falciparum-infected human erythrocytes
    • Staines, H.M.; Dee, B.C.; O'Brien, M.; Lang, H.J.; Englert, H.; Horner, H.A.; Ellory, J.C.; Kirk, K. Furosemide analogues as potent inhibitors of the new permeability pathways of Plasmodium falciparum-infected human erythrocytes. Mol. Biochem. Parasitol., 2004, 133(2), 315-318.
    • (2004) Mol. Biochem. Parasitol. , vol.133 , Issue.2 , pp. 315-318
    • Staines, H.M.1    Dee, B.C.2    O'Brien, M.3    Lang, H.J.4    Englert, H.5    Horner, H.A.6    Ellory, J.C.7    Kirk, K.8
  • 94
    • 0027134727 scopus 로고
    • Phloridzin and phloretin inhibition of 2-deoxy-D-glucose uptake by tumor cells in vitro and in vivo
    • Nelson, J.A.; Falk, R.E. Phloridzin and phloretin inhibition of 2-deoxy-D-glucose uptake by tumor cells in vitro and in vivo. Anticancer Res., 1993, 13(6A), 2293-2299.
    • (1993) Anticancer Res. , vol.13 , Issue.6 A , pp. 2293-2299
    • Nelson, J.A.1    Falk, R.E.2
  • 95
    • 0023722403 scopus 로고
    • L(+)-lactate transport in perfused rat skeletal muscle: Kinetic characteristics and sensitivity to pH and transport inhibitors
    • Watt, P.W.; MacLennan, P.A.; Hundal, H.S.; Kuret, C.M.; Rennie, M.J. L(+)-lactate transport in perfused rat skeletal muscle: kinetic characteristics and sensitivity to pH and transport inhibitors. Biochim. Biophys. Acta, 1988, 944(2), 213-222.
    • (1988) Biochim. Biophys. Acta , vol.944 , Issue.2 , pp. 213-222
    • Watt, P.W.1    MacLennan, P.A.2    Hundal, H.S.3    Kuret, C.M.4    Rennie, M.J.5
  • 96
    • 0034739003 scopus 로고    scopus 로고
    • A voltage-dependent channel involved in nutrient uptake by red blood cells infected with the malaria parasite
    • Desai, S.A.; Bezrukov, S.M.; Zimmerberg, J. A voltage-dependent channel involved in nutrient uptake by red blood cells infected with the malaria parasite. Nature, 2000, 406(6799), 1001-1005.
    • (2000) Nature , vol.406 , Issue.6799 , pp. 1001-1005
    • Desai, S.A.1    Bezrukov, S.M.2    Zimmerberg, J.3
  • 97
    • 33846032314 scopus 로고    scopus 로고
    • Targeting nutrient uptake mechanisms in Plasmodium
    • Kirk, K.; Saliba, K.J. Targeting nutrient uptake mechanisms in Plasmodium. Curr. Drug Targets, 2007, 8(1), 75-88.
    • (2007) Curr. Drug Targets , vol.8 , Issue.1 , pp. 75-88
    • Kirk, K.1    Saliba, K.J.2
  • 98
    • 24144480800 scopus 로고    scopus 로고
    • The 'permeome' of the malaria parasite: An overview of the membrane transport proteins of Plasmodium falciparum
    • Martin, R.E.; Henry, R.I.; Abbey, J.L.; Clements, J.D.; Kirk, K. The 'permeome' of the malaria parasite: an overview of the membrane transport proteins of Plasmodium falciparum. Genome Biol., 2005, 6(3), R26.
    • (2005) Genome Biol. , vol.6 , Issue.3
    • Martin, R.E.1    Henry, R.I.2    Abbey, J.L.3    Clements, J.D.4    Kirk, K.5
  • 99
    • 0034991277 scopus 로고    scopus 로고
    • Perturbation of the pump-leak balance for Na+ and K+ in malaria-infected erythrocytes
    • Staines, H.M.; Ellory, J.C.; Kirk, K. Perturbation of the pump-leak balance for Na+ and K+ in malaria-infected erythrocytes. Am. J. Physiol. Cell Physiol., 2001, 280(6), C1576-1587.
    • (2001) Am. J. Physiol. Cell Physiol. , vol.280 , Issue.6
    • Staines, H.M.1    Ellory, J.C.2    Kirk, K.3
  • 100
    • 0022378463 scopus 로고
    • The properties and regulation of pantothenate kinase from rat heart
    • Fisher, M.N.; Robishaw, J.D.; Neely, J.R. The properties and regulation of pantothenate kinase from rat heart. J. Biol. Chem., 1985, 260(29), 15745-15751.
    • (1985) J. Biol. Chem. , vol.260 , Issue.29 , pp. 15745-15751
    • Fisher, M.N.1    Robishaw, J.D.2    Neely, J.R.3
  • 101
    • 0020130867 scopus 로고
    • Regulation of the biosynthesis of CoA at the level of pantothenate kinase
    • Halvorsen, O.; Skrede, S. Regulation of the biosynthesis of CoA at the level of pantothenate kinase. Eur. J. Biochem., 1982, 124(1), 211-215.
    • (1982) Eur. J. Biochem. , vol.124 , Issue.1 , pp. 211-215
    • Halvorsen, O.1    Skrede, S.2
  • 102
    • 25444432519 scopus 로고    scopus 로고
    • Feedback regulation of murine pantothenate kinase 3 by coenzyme A and coenzyme A thioesters
    • Zhang, Y.M.; Rock, C.O.; Jackowski, S. Feedback regulation of murine pantothenate kinase 3 by coenzyme A and coenzyme A thioesters. J. Biol. Chem., 2005, 280(38), 32594-32601.
    • (2005) J. Biol. Chem. , vol.280 , Issue.38 , pp. 32594-32601
    • Zhang, Y.M.1    Rock, C.O.2    Jackowski, S.3
  • 103
    • 33644864274 scopus 로고    scopus 로고
    • Biochemical properties of human pantothenate kinase 2 isoforms and mutations linked to pantothenate kinase-associated neurodegeneration
    • Zhang, Y.M.; Rock, C.O.; Jackowski, S. Biochemical properties of human pantothenate kinase 2 isoforms and mutations linked to pantothenate kinase-associated neurodegeneration. J. Biol. Chem., 2006, 281(1), 107-114.
    • (2006) J. Biol. Chem. , vol.281 , Issue.1 , pp. 107-114
    • Zhang, Y.M.1    Rock, C.O.2    Jackowski, S.3
  • 104
    • 13544275017 scopus 로고    scopus 로고
    • A pantothenate kinase from Staphylococcus aureus refractory to feedback regulation by coenzyme A
    • Leonardi, R.; Chohnan, S.; Zhang, Y.M.; Virga, K.G.; Lee, R.E.; Rock, C.O.; Jackowski, S. A pantothenate kinase from Staphylococcus aureus refractory to feedback regulation by coenzyme A. J. Biol. Chem., 2005, 280(5), 3314-3322.
    • (2005) J. Biol. Chem. , vol.280 , Issue.5 , pp. 3314-3322
    • Leonardi, R.1    Chohnan, S.2    Zhang, Y.M.3    Virga, K.G.4    Lee, R.E.5    Rock, C.O.6    Jackowski, S.7
  • 105
    • 0037073693 scopus 로고    scopus 로고
    • The antibiotic activity of Npentylpantothenamide results from its conversion to ethyldethiacoenzyme A, a coenzyme A antimetabolite
    • Strauss, E.; Begley, T.P. The antibiotic activity of Npentylpantothenamide results from its conversion to ethyldethiacoenzyme A, a coenzyme A antimetabolite. J. Biol. Chem., 2002, 277(50), 48205-48209.
    • (2002) J. Biol. Chem. , vol.277 , Issue.50 , pp. 48205-48209
    • Strauss, E.1    Begley, T.P.2
  • 106
    • 10944262320 scopus 로고    scopus 로고
    • Acyl carrier protein is a cellular target for the antibacterial action of the pantothenamide class of pantothenate antimetabolites
    • Zhang, Y.M.; Frank, M.W.; Virga, K.G.; Lee, R.E.; Rock, C.O.; Jackowski, S. Acyl carrier protein is a cellular target for the antibacterial action of the pantothenamide class of pantothenate antimetabolites. J. Biol. Chem., 2004, 279(49), 50969-50975.
    • (2004) J. Biol. Chem. , vol.279 , Issue.49 , pp. 50969-50975
    • Zhang, Y.M.1    Frank, M.W.2    Virga, K.G.3    Lee, R.E.4    Rock, C.O.5    Jackowski, S.6
  • 107
    • 34547856677 scopus 로고    scopus 로고
    • How pantothenol intervenes in Coenzyme-A biosynthesis of Mycobacterium tuberculosis
    • Kumar, P.; Chhibber, M.; Surolia, A. How pantothenol intervenes in Coenzyme-A biosynthesis of Mycobacterium tuberculosis. Biochem. Biophys. Res. Commun., 2007, 361(4), 903-909.
    • (2007) Biochem. Biophys. Res. Commun. , vol.361 , Issue.4 , pp. 903-909
    • Kumar, P.1    Chhibber, M.2    Surolia, A.3
  • 108
    • 3042591086 scopus 로고    scopus 로고
    • Coenzyme A biosynthesis: Reconstruction of the pathway in archaea and an evolutionary scenario based on comparative genomics
    • Genschel, U. Coenzyme A biosynthesis: reconstruction of the pathway in archaea and an evolutionary scenario based on comparative genomics. Mol. Biol. Evol., 2004, 21(7), 1242-1251.
    • (2004) Mol. Biol. Evol. , vol.21 , Issue.7 , pp. 1242-1251
    • Genschel, U.1
  • 109
    • 33746822335 scopus 로고    scopus 로고
    • Prokaryotic type II and type III pantothenate kinases: The same monomer fold creates dimers with distinct catalytic properties
    • Hong, B.S.; Yun, M.K.; Zhang, Y.M.; Chohnan, S.; Rock, C.O.; White, S.W.; Jackowski, S.; Park, H.W.; Leonardi, R. Prokaryotic type II and type III pantothenate kinases: The same monomer fold creates dimers with distinct catalytic properties. Structure, 2006, 14(8), 1251-1261.
    • (2006) Structure , vol.14 , Issue.8 , pp. 1251-1261
    • Hong, B.S.1    Yun, M.K.2    Zhang, Y.M.3    Chohnan, S.4    Rock, C.O.5    White, S.W.6    Jackowski, S.7    Park, H.W.8    Leonardi, R.9
  • 110
    • 33746614112 scopus 로고    scopus 로고
    • Crystal structure of a type III pantothenate kinase: Insight into the mechanism of an essential coenzyme A biosynthetic enzyme universally distributed in bacteria
    • Yang, K.; Eyobo, Y.; Brand, L.A.; Martynowski, D.; Tomchick, D.; Strauss, E.; Zhang, H. Crystal structure of a type III pantothenate kinase: Insight into the mechanism of an essential coenzyme A biosynthetic enzyme universally distributed in bacteria. J. Bacteriol., 2006, 188(15), 5532-5540.
    • (2006) J. Bacteriol. , vol.188 , Issue.15 , pp. 5532-5540
    • Yang, K.1    Eyobo, Y.2    Brand, L.A.3    Martynowski, D.4    Tomchick, D.5    Strauss, E.6    Zhang, H.7
  • 111
    • 34948897631 scopus 로고    scopus 로고
    • Crystal structures of human pantothenate kinases. Insights into allosteric regulation and mutations linked to a neurodegeneration disorder
    • Hong, B.S.; Senisterra, G.; Rabeh, W.M.; Vedadi, M.; Leonardi, R.; Zhang, Y.M.; Rock, C.O.; Jackowski, S.; Park, H.W. Crystal structures of human pantothenate kinases. Insights into allosteric regulation and mutations linked to a neurodegeneration disorder. J. Biol. Chem., 2007, 282(38), 27984-27993.
    • (2007) J. Biol. Chem. , vol.282 , Issue.38 , pp. 27984-27993
    • Hong, B.S.1    Senisterra, G.2    Rabeh, W.M.3    Vedadi, M.4    Leonardi, R.5    Zhang, Y.M.6    Rock, C.O.7    Jackowski, S.8    Park, H.W.9
  • 112
    • 17844401480 scopus 로고    scopus 로고
    • A comprehensive update of the sequence and structure classification of kinases
    • Cheek, S.; Ginalski, K.; Zhang, H.; Grishin, N.V. A comprehensive update of the sequence and structure classification of kinases. BMC Struct. Biol., 2005, 5, 6.
    • (2005) BMC Struct. Biol. , vol.5 , pp. 6
    • Cheek, S.1    Ginalski, K.2    Zhang, H.3    Grishin, N.V.4
  • 113
    • 0036305943 scopus 로고    scopus 로고
    • Sequence and structure classification of kinases
    • Cheek, S.; Zhang, H.; Grishin, N.V. Sequence and structure classification of kinases. J. Mol. Biol., 2002, 320(4), 855-881.
    • (2002) J. Mol. Biol. , vol.320 , Issue.4 , pp. 855-881
    • Cheek, S.1    Zhang, H.2    Grishin, N.V.3
  • 114
    • 0035104190 scopus 로고    scopus 로고
    • Low-complexity regions in Plasmodium falciparum proteins
    • Pizzi, E.; Frontali, C. Low-complexity regions in Plasmodium falciparum proteins. Genome Res., 2001, 11(2), 218-229.
    • (2001) Genome Res. , vol.11 , Issue.2 , pp. 218-229
    • Pizzi, E.1    Frontali, C.2
  • 115
    • 4644370187 scopus 로고    scopus 로고
    • Hyper-expansion of asparagines correlates with an abundance of proteins with prion-like domains in Plasmodium falciparum
    • Singh, G.P.; Chandra, B.R.; Bhattacharya, A.; Akhouri, R.R.; Singh, S.K.; Sharma, A. Hyper-expansion of asparagines correlates with an abundance of proteins with prion-like domains in Plasmodium falciparum. Mol. Biochem. Parasitol., 2004, 137(2), 307-319.
    • (2004) Mol. Biochem. Parasitol. , vol.137 , Issue.2 , pp. 307-319
    • Singh, G.P.1    Chandra, B.R.2    Bhattacharya, A.3    Akhouri, R.R.4    Singh, S.K.5    Sharma, A.6
  • 118
    • 43249103226 scopus 로고    scopus 로고
    • Cloning and confirmation of several potential pantothenate kinases which display different specificities for pantothenate analogues
    • Shen, D.; Huang, Q.; Sha, Y.; Bing, Z. Cloning and confirmation of several potential pantothenate kinases which display different specificities for pantothenate analogues. J. Tsinghua Univ., 2008, 48(3), 403-407.
    • (2008) J. Tsinghua Univ. , vol.48 , Issue.3 , pp. 403-407
    • Shen, D.1    Huang, Q.2    Sha, Y.3    Bing, Z.4
  • 119
    • 0001960537 scopus 로고
    • Determination of Blood Sugar
    • Somogyi, M. Determination of Blood Sugar. J. Biol. Chem., 1945, 160(1), 69-73.
    • (1945) J. Biol. Chem. , vol.160 , Issue.1 , pp. 69-73
    • Somogyi, M.1
  • 120
    • 4143098353 scopus 로고    scopus 로고
    • The structure of the pantothenate kinase.ADP.pantothenate ternary complex reveals the relationship between the binding sites for substrate, allosteric regulator, and antimetabolites
    • Ivey, R.A.; Zhang, Y.M.; Virga, K.G.; Hevener, K.; Lee, R.E.; Rock, C.O.; Jackowski, S.; Park, H.W. The structure of the pantothenate kinase.ADP.pantothenate ternary complex reveals the relationship between the binding sites for substrate, allosteric regulator, and antimetabolites. J. Biol. Chem., 2004, 279(34), 35622-35629.
    • (2004) J. Biol. Chem. , vol.279 , Issue.34 , pp. 35622-35629
    • Ivey, R.A.1    Zhang, Y.M.2    Virga, K.G.3    Hevener, K.4    Lee, R.E.5    Rock, C.O.6    Jackowski, S.7    Park, H.W.8
  • 121
    • 54349125693 scopus 로고    scopus 로고
    • The inhibitory effect of 2-halo derivatives of D-glucose on glycolysis and on the proliferation of the human malaria parasite Plasmodium falciparum
    • van Schalkwyk, D.A.; Priebe, W.; Saliba, K.J. The inhibitory effect of 2-halo derivatives of D-glucose on glycolysis and on the proliferation of the human malaria parasite Plasmodium falciparum. J. Pharmacol. Exp. Ther., 2008, 327(2), 511-517.
    • (2008) J. Pharmacol. Exp. Ther. , vol.327 , Issue.2 , pp. 511-517
    • van Schalkwyk, D.A.1    Priebe, W.2    Saliba, K.J.3
  • 122
    • 55249093843 scopus 로고    scopus 로고
    • Antibiotic evaluation and in vivo analysis of alkynyl Coenzyme A antimetabolites in Escherichia coli
    • Mercer, A.C.; Meier, J.L.; Hur, G.H.; Smith, A.R.; Burkart, M.D. Antibiotic evaluation and in vivo analysis of alkynyl Coenzyme A antimetabolites in Escherichia coli. Bioorg. Med. Chem. Lett., 2008, 18(22), 5991-5994.
    • (2008) Bioorg. Med. Chem. Lett. , vol.18 , Issue.22 , pp. 5991-5994
    • Mercer, A.C.1    Meier, J.L.2    Hur, G.H.3    Smith, A.R.4    Burkart, M.D.5
  • 123
    • 0033954772 scopus 로고    scopus 로고
    • Pantothenate kinase regulation of the intracellular concentration of coenzyme A
    • Rock, C.O.; Calder, R.B.; Karim, M.A.; Jackowski, S. Pantothenate kinase regulation of the intracellular concentration of coenzyme A. J. Biol. Chem., 2000, 275(2), 1377-1383.
    • (2000) J. Biol. Chem. , vol.275 , Issue.2 , pp. 1377-1383
    • Rock, C.O.1    Calder, R.B.2    Karim, M.A.3    Jackowski, S.4
  • 124
    • 14844349363 scopus 로고    scopus 로고
    • metaSHARK: Software for automated metabolic network prediction from DNA sequence and its application to the genomes of Plasmodium falciparum and Eimeria tenella
    • Pinney, J.W.; Shirley, M.W.; McConkey, G.A.; Westhead, D.R. metaSHARK: software for automated metabolic network prediction from DNA sequence and its application to the genomes of Plasmodium falciparum and Eimeria tenella. Nucleic Acids Res., 2005, 33(4), 1399-1409.
    • (2005) Nucleic Acids Res. , vol.33 , Issue.4 , pp. 1399-1409
    • Pinney, J.W.1    Shirley, M.W.2    McConkey, G.A.3    Westhead, D.R.4
  • 127
    • 0033578920 scopus 로고    scopus 로고
    • Purification and characterization of phosphopantetheine adenylyltransferase from Escherichia coli
    • Geerlof, A.; Lewendon, A.; Shaw, W.V. Purification and characterization of phosphopantetheine adenylyltransferase from Escherichia coli. J. Biol. Chem., 1999, 274(38), 27105-27111.
    • (1999) J. Biol. Chem. , vol.274 , Issue.38 , pp. 27105-27111
    • Geerlof, A.1    Lewendon, A.2    Shaw, W.V.3
  • 128
    • 0035920198 scopus 로고    scopus 로고
    • Molecular characterization of the 4'-phosphopantothenoylcysteine decarboxylase domain of bacterial Dfp flavoproteins
    • Kupke, T. Molecular characterization of the 4'-phosphopantothenoylcysteine decarboxylase domain of bacterial Dfp flavoproteins. J. Biol. Chem., 2001, 276(29), 27597-27604.
    • (2001) J. Biol. Chem. , vol.276 , Issue.29 , pp. 27597-27604
    • Kupke, T.1
  • 129
    • 0037184111 scopus 로고    scopus 로고
    • Molecular characterization of the 4'-phosphopantothenoylcysteine synthetase domain of bacterial Dfp flavoproteins
    • Kupke, T. Molecular characterization of the 4'-phosphopantothenoylcysteine synthetase domain of bacterial Dfp flavoproteins. J. Biol. Chem., 2002, 277(39), 36137-36145.
    • (2002) J. Biol. Chem. , vol.277 , Issue.39 , pp. 36137-36145
    • Kupke, T.1
  • 130
    • 0035046479 scopus 로고    scopus 로고
    • Identification of yacE (coaE) as the structural gene for dephosphocoenzyme A kinase in Escherichia coli K-12
    • Mishra, P.; Park, P.K.; Drueckhammer, D.G. Identification of yacE (coaE) as the structural gene for dephosphocoenzyme A kinase in Escherichia coli K-12. J. Bacteriol., 2001, 183(9), 2774-2778.
    • (2001) J. Bacteriol. , vol.183 , Issue.9 , pp. 2774-2778
    • Mishra, P.1    Park, P.K.2    Drueckhammer, D.G.3
  • 133
    • 0041663296 scopus 로고    scopus 로고
    • Structure of human phosphopantothenoylcysteine synthetase at 2.3 Å resolution
    • Manoj, N.; Strauss, E.; Begley, T.P.; Ealick, S.E. Structure of human phosphopantothenoylcysteine synthetase at 2.3 Å resolution. Structure, 2003, 11(8), 927-936.
    • (2003) Structure , vol.11 , Issue.8 , pp. 927-936
    • Manoj, N.1    Strauss, E.2    Begley, T.P.3    Ealick, S.E.4
  • 134
    • 56349093395 scopus 로고    scopus 로고
    • Development of a method for the parallel synthesis and purification of N-substituted pantothenamides, known inhibitors of coenzyme A biosynthesis and utilization
    • van Wyk, M.; Strauss, E. Development of a method for the parallel synthesis and purification of N-substituted pantothenamides, known inhibitors of coenzyme A biosynthesis and utilization. Org. Biomol. Chem., 2008, 6(23), 4348-4355.
    • (2008) Org. Biomol. Chem. , vol.6 , Issue.23 , pp. 4348-4355
    • van Wyk, M.1    Strauss, E.2
  • 136
    • 33947435662 scopus 로고
    • The synthesis of potential antimalarials - the preparation of methylated amides of taurine and their pantoyl derivatives
    • Mead, J.F.; Koepfli, J.B. The synthesis of potential antimalarials - the preparation of methylated amides of taurine and their pantoyl derivatives. J. Org. Chem., 1947, 12(2), 295-297.
    • (1947) J. Org. Chem. , vol.12 , Issue.2 , pp. 295-297
    • Mead, J.F.1    Koepfli, J.B.2
  • 137
    • 11144349367 scopus 로고
    • The synthesis of potential antimalarials - derivatives of pantoyltaurine
    • Mead, J.F.; Rapport, M.M.; Senear, A.E.; Maynard, J.T.; Koepfli, J.B. The synthesis of potential antimalarials - derivatives of pantoyltaurine. J. Biol. Chem., 1946, 163(2), 465-473.
    • (1946) J. Biol. Chem. , vol.163 , Issue.2 , pp. 465-473
    • Mead, J.F.1    Rapport, M.M.2    Senear, A.E.3    Maynard, J.T.4    Koepfli, J.B.5
  • 138
    • 13344268531 scopus 로고
    • Summary of data on the drugs tested in man
    • In: Wiselogle F.Y., Ed.; J. W. Edwards: Michigan
    • Berliner, R.W.; Butler, T.C. Summary of data on the drugs tested in man. In: A survey of antimalarial drugs 1941-1945; Wiselogle, F.Y., Ed.; J. W. Edwards: Michigan, 1946; pp. 221-451.
    • (1946) A survey of antimalarial drugs 1941-1945 , pp. 221-451
    • Berliner, R.W.1    Butler, T.C.2
  • 139
    • 0015063468 scopus 로고
    • Further studies on the effects of antipantothenates on malaria parasites (Plasmodium coatneyi and P. falciparum) in vitro
    • Trager, W. Further studies on the effects of antipantothenates on malaria parasites (Plasmodium coatneyi and P. falciparum) in vitro. J. Protozool., 1971, 18(2), 232-239.
    • (1971) J. Protozool. , vol.18 , Issue.2 , pp. 232-239
    • Trager, W.1
  • 140
    • 42449090264 scopus 로고    scopus 로고
    • PROMALS3D: A tool for multiple protein sequence and structure alignments
    • Pei, J.; Kim, B.H.; Grishin, N.V. PROMALS3D: a tool for multiple protein sequence and structure alignments. Nucleic Acids Res., 2008, 36(7), 2295-2300.
    • (2008) Nucleic Acids Res. , vol.36 , Issue.7 , pp. 2295-2300
    • Pei, J.1    Kim, B.H.2    Grishin, N.V.3
  • 141
    • 0035747672 scopus 로고    scopus 로고
    • Enhancement of protein modeling by human intervention in applying the automatic programs 3D-JIGSAW and 3D-PSSM
    • Bates, P.A.; Kelley, L.A.; MacCallum, R.M.; Sternberg, M.J. Enhancement of protein modeling by human intervention in applying the automatic programs 3D-JIGSAW and 3D-PSSM. Proteins, 2001, (Suppl. 5), 39-46.
    • (2001) Proteins , Issue.SUPPL. 5 , pp. 39-46
    • Bates, P.A.1    Kelley, L.A.2    MacCallum, R.M.3    Sternberg, M.J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.