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Volumn 17, Issue 4, 2012, Pages 634-656

The use and abuse of heme in apicomplexan parasites

Author keywords

[No Author keywords available]

Indexed keywords

CATALASE; CYTOCHROME B; CYTOCHROME B5; CYTOCHROME C; CYTOCHROME C1; CYTOCHROME C2; CYTOCHROME P450; GLOBIN; HEME; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE; TETRAPYRROLE DERIVATIVE;

EID: 84862533617     PISSN: 15230864     EISSN: 15577716     Source Type: Journal    
DOI: 10.1089/ars.2012.4539     Document Type: Review
Times cited : (58)

References (181)
  • 2
    • 0037047370 scopus 로고    scopus 로고
    • Trans expression of a Plasmodium falciparum histidine-rich protein II (HRPII) reveals sorting of soluble proteins in the periphery of the host erythrocyte and disrupts transport to the malarial food vacuole
    • Akompong T, Kadekoppala M, Harrison T, Oksman A, Goldberg DE, Fujioka H, Samuel BU, Sullivan D, and Haldar K. Trans expression of a Plasmodium falciparum histidine-rich protein II (HRPII) reveals sorting of soluble proteins in the periphery of the host erythrocyte and disrupts transport to the malarial food vacuole. J Biol Chem 277: 28923-28933, 2002.
    • (2002) J Biol Chem , vol.277 , pp. 28923-28933
    • Akompong, T.1    Kadekoppala, M.2    Harrison, T.3    Oksman, A.4    Goldberg, D.E.5    Fujioka, H.6    Samuel, B.U.7    Sullivan, D.8    Haldar, K.9
  • 3
    • 0029933923 scopus 로고    scopus 로고
    • Free-radical-induced mutation vs redox regulation: Costs and benefits of genes in organelles
    • DOI 10.1007/BF02352278
    • Allen JF and Raven JA. Free-radical-induced mutation vs redox regulation: costs and benefits of genes in organelles. J Mol Evol 42: 482-492, 1996. (Pubitemid 26197138)
    • (1996) Journal of Molecular Evolution , vol.42 , Issue.5 , pp. 482-492
    • Allen, J.F.1    Raven, J.A.2
  • 5
    • 78649921851 scopus 로고    scopus 로고
    • Overcoming the heme paradox: Heme toxicity and tolerance in bacterial pathogens
    • Anzaldi LL and Skaar EP. Overcoming the heme paradox: heme toxicity and tolerance in bacterial pathogens. Infect Immun 78: 4977-4989, 2010.
    • (2010) Infect Immun , vol.78 , pp. 4977-4989
    • Anzaldi, L.L.1    Skaar, E.P.2
  • 6
    • 0026073466 scopus 로고
    • Remarkable in vitro and in vivo activities of the hydroxynaphthoquinone 566C80 against tachyzoites and tissue cysts of Toxoplasma gondii
    • Araujo FG, Huskinson J, and Remington JS. Remarkable in vitro and in vivo activities of the hydroxynaphthoquinone 566C80 against tachyzoites and tissue cysts of Toxoplasma gondii. Antimicrob Agents Chemother 35: 293-299, 1991.
    • (1991) Antimicrob Agents Chemother , vol.35 , pp. 293-299
    • Araujo, F.G.1    Huskinson, J.2    Remington, J.S.3
  • 7
    • 84862580459 scopus 로고    scopus 로고
    • Inherited disorders of haem synthesis: The human porphyrias
    • edited by Warren MJ and Smith AG. Austin: Landes Bioscience
    • Badminton MN and Elder GH. Inherited disorders of haem synthesis: the human porphyrias. In: Tetrapyrroles: Birth, Life and Death, edited by Warren MJ and Smith AG. Austin: Landes Bioscience, 2009, pp. 89-100.
    • (2009) Tetrapyrroles: Birth, Life and Death , pp. 89-100
    • Badminton, M.N.1    Elder, G.H.2
  • 8
    • 82355181574 scopus 로고    scopus 로고
    • ATP synthase complex of Plasmodium falciparum: Dimeric assembly in mitochondrial membranes and resistance to genetic disruption
    • Balabaskaran Nina P, Morrisey JM, Ganesan SM, Ke H, Pershing AM, Mather MW, and Vaidya AB. ATP synthase complex of Plasmodium falciparum: dimeric assembly in mitochondrial membranes and resistance to genetic disruption. J Biol Chem 286: 41312-41322, 2011.
    • (2011) J Biol Chem , vol.286 , pp. 41312-41322
    • Balabaskaran Nina, P.1    Morrisey, J.M.2    Ganesan, S.M.3    Ke, H.4    Pershing, A.M.5    Mather, M.W.6    Vaidya, A.B.7
  • 9
    • 0015619867 scopus 로고
    • 14C incorporation from exogenous compounds into d-aminolevulinic acid by greening cucumber cotyledons
    • Beale SI and Castelfranco PA. 14C incorporation from exogenous compounds into d-aminolevulinic acid by greening cucumber cotyledons. Biochem Biophys Res Commun 52: 143-149, 1973.
    • (1973) Biochem Biophys Res Commun , vol.52 , pp. 143-149
    • Beale, S.I.1    Castelfranco, P.A.2
  • 10
    • 33646446147 scopus 로고    scopus 로고
    • Functional characterization and target validation of alternative complex I of Plasmodium falciparum mitochondria
    • Biagini GA, Viriyavejakul P, O'Neill PM, Bray PG, and Ward SA. Functional characterization and target validation of alternative complex I of Plasmodium falciparum mitochondria. Antimicrob Agents Chemother 50: 1841-1851, 2006.
    • (2006) Antimicrob Agents Chemother , vol.50 , pp. 1841-1851
    • Biagini, G.A.1    Viriyavejakul, P.2    O'Neill, P.M.3    Bray, P.G.4    Ward, S.A.5
  • 11
    • 0033834719 scopus 로고    scopus 로고
    • Import of host delta-aminolevulinate dehydratase into the malarial parasite: Identification of a new drug target
    • DOI 10.1038/78659
    • Bonday ZQ, Dhanasekaran S, Rangarajan PN, and Padmanaban G. Import of host delta-aminolevulinate dehydratase into the malarial parasite: identification of a new drug target. Nat Med 6: 898-903, 2000. (Pubitemid 30644748)
    • (2000) Nature Medicine , vol.6 , Issue.8 , pp. 898-903
    • Bonday, Z.Q.1    Dhanasekaran, S.2    Rangarajan, P.N.3    Padmanaban, G.4
  • 12
    • 0030758361 scopus 로고    scopus 로고
    • Heme biosynthesis by the malarial parasite: Import of delta- aminolevulinate dehydrase from the host red cell
    • DOI 10.1074/jbc.272.35.21839
    • Bonday ZQ, Taketani S, Gupta PD, and Padmanaban G. Heme biosynthesis by the malarial parasite. Import of delta-aminolevulinate dehydrase from the host red cell. J Biol Chem 272: 21839-21846, 1997. (Pubitemid 27382800)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.35 , pp. 21839-21846
    • Bonday, Z.Q.1    Taketani, S.2    Gupta, P.D.3    Padmanaban, G.4
  • 13
    • 80053929001 scopus 로고    scopus 로고
    • Comparison of the reactivity of antimalarial 1,2,4,5-tetraoxanes with 1,2,4-trioxolanes in the presence of ferrous iron salts, heme, and ferrous iron salts/ phosphatidylcholine
    • Bousejra-El Garah F, Wong MH, Amewu RK, Muangnoicharoen S, Maggs JL, Stigliani JL, Park BK, Chadwick J, Ward SA, and O'Neill PM. Comparison of the reactivity of antimalarial 1,2,4,5-tetraoxanes with 1,2,4-trioxolanes in the presence of ferrous iron salts, heme, and ferrous iron salts/ phosphatidylcholine. J Med Chem 54: 6443-6455, 2011.
    • (2011) J Med Chem , vol.54 , pp. 6443-6455
    • Bousejra-El Garah, F.1    Wong, M.H.2    Amewu, R.K.3    Muangnoicharoen, S.4    Maggs, J.L.5    Stigliani, J.L.6    Park, B.K.7    Chadwick, J.8    Ward, S.A.9    O'Neill, P.M.10
  • 14
    • 80052695300 scopus 로고    scopus 로고
    • Arrested oocyst maturation in Plasmodium parasites lacking type II NADH: Ubiquinone dehydrogenase
    • Boysen KE and Matuschewski K. Arrested oocyst maturation in Plasmodium parasites lacking type II NADH: ubiquinone dehydrogenase. J Biol Chem 286: 32661-32671, 2011.
    • (2011) J Biol Chem , vol.286 , pp. 32661-32671
    • Boysen, K.E.1    Matuschewski, K.2
  • 15
    • 0023040126 scopus 로고
    • Purification and properties of coproporphyrinogen oxidase from the yeast Saccharomyces cerevisiae
    • Camadro JM, Chambon H, Jolles J, and Labbe P. Purification and properties of coproporphyrinogen oxidase from the yeast Saccharomyces cerevisiae. Eur J Biochem 156: 579-587, 1986.
    • (1986) Eur J Biochem , vol.156 , pp. 579-587
    • Camadro, J.M.1    Chambon, H.2    Jolles, J.3    Labbe, P.4
  • 17
    • 0036496185 scopus 로고    scopus 로고
    • 0-type ATP synthase, a biological rotary motor
    • DOI 10.1016/S0968-0004(01)02051-5, PII S0968000401020515
    • Capaldi RA and Aggeler R. Mechanism of the F(1)F(0)-type ATP synthase, a biological rotary motor. Trends Biochem Sci 27: 154-160, 2002. (Pubitemid 34219326)
    • (2002) Trends in Biochemical Sciences , vol.27 , Issue.3 , pp. 154-160
    • Capaldi, R.A.1    Aggeler, R.2
  • 19
    • 0015947565 scopus 로고
    • Nutritional significance of symbiotic bacteria in two species of hemoflagellates
    • Chang KP and Trager W. Nutritional significance of symbiotic bacteria in two species of hemoflagellates. Science 183: 531-532, 1974.
    • (1974) Science , vol.183 , pp. 531-532
    • Chang, K.P.1    Trager, W.2
  • 20
    • 77956044833 scopus 로고    scopus 로고
    • Ferrochelatase forms an oligomeric complex with mitoferrin-1 and Abcb10 for erythroid heme biosynthesis
    • Chen W, Dailey HA, and Paw BH. Ferrochelatase forms an oligomeric complex with mitoferrin-1 and Abcb10 for erythroid heme biosynthesis. Blood 116: 628-630, 2010.
    • (2010) Blood , vol.116 , pp. 628-630
    • Chen, W.1    Dailey, H.A.2    Paw, B.H.3
  • 21
    • 0036499460 scopus 로고    scopus 로고
    • Measurement of ferrochelatase activity using a novel assay suggests that plastids are the major site of haem biosynthesis in both photosynthetic and non-photosynthetic cells of pea (Pisum sativum L.)
    • DOI 10.1042/0264-6021:3620423
    • Cornah JE, Roper JM, Pal Singh D, and Smith AG. Measurement of ferrochelatase activity using a novel assay suggests that plastids are the major site of haem biosynthesis in both photosynthetic and non-photosynthetic cells of pea (Pisum sativum L.). Biochem J 362: 423-432, 2002. (Pubitemid 34214485)
    • (2002) Biochemical Journal , vol.362 , Issue.2 , pp. 423-432
    • Cornah, J.E.1    Roper, J.M.2    Singh, D.P.3    Smith, A.G.4
  • 22
    • 77952721867 scopus 로고    scopus 로고
    • Transformation of uroporphyrinogen III into protohaem
    • edited by Warren MJ and Smith AG. Austin: Landes Bioscience
    • Cornah JE and Smith AG. Transformation of uroporphyrinogen III into protohaem. In: Tetrapyrroles: Birth, Life and Death, edited by Warren MJ and Smith AG. Austin: Landes Bioscience, 2009, pp. 74-88.
    • (2009) Tetrapyrroles: Birth, Life and Death , pp. 74-88
    • Cornah, J.E.1    Smith, A.G.2
  • 23
    • 0025786518 scopus 로고
    • A P-glycoprotein homologue of Plasmodium falciparum is localized on the digestive vacuole
    • Cowman AF, Karcz S, Galatis D, and Culvenor JG. A P-glycoprotein homologue of Plasmodium falciparum is localized on the digestive vacuole. J Cell Biol 113: 1033-1042, 1991. (Pubitemid 21909736)
    • (1991) Journal of Cell Biology , vol.113 , Issue.5 , pp. 1033-1042
    • Cowman, A.F.1    Karcz, S.2    Galatis, D.3    Culvenor, J.G.4
  • 24
    • 1942447877 scopus 로고    scopus 로고
    • 1 complex: Function in the context of structure
    • DOI 10.1146/annurev.physiol.66.032102.150251
    • Crofts AR. The cytochrome bc1 complex: function in the context of structure. Annu Rev Physiol 66: 689-733, 2004. (Pubitemid 40614460)
    • (2004) Annual Review of Physiology , vol.66 , pp. 689-733
    • Crofts, A.R.1
  • 28
  • 29
    • 0347595338 scopus 로고    scopus 로고
    • The antioxidant systems in Toxoplasma gondii and the role of cytosolic catalase in defence against oxidative injury
    • DOI 10.1046/j.1365-2958.2003.03823.x
    • Ding M, Kwok LY, Schluter D, Clayton C, and Soldati D. The antioxidant systems in Toxoplasma gondii and the role of cytosolic catalase in defence against oxidative injury. Mol Microbiol 51: 47-61, 2004. (Pubitemid 38031070)
    • (2004) Molecular Microbiology , vol.51 , Issue.1 , pp. 47-61
    • Kwok, L.Y.1    Schluter, D.2    Clayton, C.3    Soldati, D.4
  • 30
    • 0024332591 scopus 로고
    • Regulation of the stability of chicken embryo liver delta-aminolevulinate synthase mRNA by hemin
    • Drew PD and Ades IZ. Regulation of the stability of chicken embryo liver delta-aminolevulinate synthase mRNA by hemin. Biochem Biophys Res Commun 162: 102-107, 1989. (Pubitemid 19185833)
    • (1989) Biochemical and Biophysical Research Communications , vol.162 , Issue.1 , pp. 102-107
    • Drew, P.D.1    Ades, I.Z.2
  • 32
    • 0030870923 scopus 로고    scopus 로고
    • Thermodynamic factors controlling the interaction of quinoline antimalarial drugs with ferriprotoporphyrin IX
    • DOI 10.1016/S0162-0134(97)00086-X, PII S016201349700086X
    • Egan TJ, Mavuso WW, Ross DC, and Marques HM. Thermodynamic factors controlling the interaction of quinoline antimalarial drugs with ferriprotoporphyrin IX. J Inorg Biochem 68: 137-145, 1997. (Pubitemid 27441170)
    • (1997) Journal of Inorganic Biochemistry , vol.68 , Issue.2 , pp. 137-145
    • Egan, T.J.1    Mavuso, W.W.2    Ross, D.C.3    Marques, H.M.4
  • 33
    • 0033527572 scopus 로고    scopus 로고
    • Identification and characterization of falcilysin, a metallopeptidase involved in hemoglobin catabolism within the malaria parasite Plasmodium falciparum
    • Eggleson KK, Duffin KL, and Goldberg DE. Identification and characterization of falcilysin, a metallopeptidase involved in hemoglobin catabolism within the malaria parasite Plasmodium falciparum. J Biol Chem 274: 32411-32417, 1999.
    • (1999) J Biol Chem , vol.274 , pp. 32411-32417
    • Eggleson, K.K.1    Duffin, K.L.2    Goldberg, D.E.3
  • 34
    • 0017811997 scopus 로고
    • Evidence that the coproporphyrinogen oxidase activity of rat liver is situated in the intermembrane space of mitochondria
    • Elder GH and Evans JO. Evidence that the coproporphyrinogen oxidase activity of rat liver is situated in the intermembrane space of mitochondria. Biochem J 172: 345-347, 1978. (Pubitemid 8332516)
    • (1978) Biochemical Journal , vol.172 , Issue.2 , pp. 345-347
    • Elder, G.H.1    Evans, J.O.2
  • 35
    • 0000021902 scopus 로고    scopus 로고
    • Heme/Copper Terminal Oxidases
    • Ferguson-Miller S and Babcock GT. Heme/Copper Terminal Oxidases. Chem Rev 96: 2889-2908, 1996.
    • (1996) Chem Rev , vol.96 , pp. 2889-2908
    • Ferguson-Miller, S.1    Babcock, G.T.2
  • 37
    • 0030879653 scopus 로고    scopus 로고
    • Hemoglobin metabolism in the malaria parasite Plasmodium falciparium
    • DOI 10.1146/annurev.micro.51.1.97
    • Francis SE, Sullivan DJ, Jr., and Goldberg DE. Hemoglobin metabolism in the malaria parasite Plasmodium falciparum. Annu Rev Microbiol 51: 97-123, 1997. (Pubitemid 27433044)
    • (1997) Annual Review of Microbiology , vol.51 , pp. 97-123
    • Francis, S.E.1    Sullivan Jr., D.J.2    Goldberg, D.E.3
  • 38
    • 0141761124 scopus 로고    scopus 로고
    • The diversity of globin-coupled sensors
    • DOI 10.1016/S0014-5793(03)00923-2
    • Freitas TA, Hou S, and Alam M. The diversity of globin-coupled sensors. FEBS Lett 552: 99-104, 2003. (Pubitemid 37186842)
    • (2003) FEBS Letters , vol.552 , Issue.2-3 , pp. 99-104
    • Freitas, T.A.K.1    Hou, S.2    Alam, M.3
  • 40
    • 0026099675 scopus 로고
    • Mitochondria of mammalian Plasmodium spp
    • Fry M and Beesley JE. Mitochondria of mammalian Plasmodium spp. Parasitology 102 Pt 1: 17-26, 1991.
    • (1991) Parasitology , vol.102 , Issue.PART 1 , pp. 17-26
    • Fry, M.1    Beesley, J.E.2
  • 42
    • 0011137620 scopus 로고
    • Initial stages in the biosynthesis of porphyrins. 2. The formation of delta-aminolaevulic acid from glycine and succinyl-coenzyme A by particles fromchicken erythrocytes
    • Gibson KD, LaverWG, and Neuberger A. Initial stages in the biosynthesis of porphyrins. 2. The formation of delta-aminolaevulic acid from glycine and succinyl-coenzyme A by particles fromchicken erythrocytes. Biochem J 70: 71-81, 1958.
    • (1958) Biochem J , vol.70 , pp. 71-81
    • Gibson, K.D.1    Laver, W.G.2    Neuberger, A.3
  • 44
    • 0018113945 scopus 로고
    • The mitochondrial localization of coproporphyrinogen III oxidase
    • Grandchamp B, Phung N, and Nordmann Y. The mitochondrial localization of coproporphyrinogen III oxidase. Biochem J 176: 97-102, 1978. (Pubitemid 9060515)
    • (1978) Biochemical Journal , vol.176 , Issue.1 , pp. 97-102
    • Grandchamp, B.1    Phung, N.2    Nordmann, Y.3
  • 45
    • 39849106369 scopus 로고    scopus 로고
    • The limits and intensity of Plasmodium falciparum transmission: Implications for malaria control and elimination worldwide
    • Guerra CA, Gikandi PW, Tatem AJ, Noor AM, Smith DL,Hay SI, and Snow RW. The limits and intensity of Plasmodium falciparum transmission: implications for malaria control and elimination worldwide. PLoS Med 5: e38, 2008.
    • (2008) PLoS Med , vol.5
    • Guerra, C.A.1    Gikandi, P.W.2    Tatem, A.J.3    Noor, A.M.4    Smith, D.L.5    Hay, S.I.6    Snow, R.W.7
  • 47
    • 0013910302 scopus 로고
    • Chloroquine resistance in Plasmodium berghei
    • Hawking F. Chloroquine resistance in Plasmodium berghei. Am J Trop Med Hyg 15: 287-293, 1966.
    • (1966) Am J Trop Med Hyg , vol.15 , pp. 287-293
    • Hawking, F.1
  • 48
    • 33645849237 scopus 로고    scopus 로고
    • Structures of the high-valent metalion haem-oxygen intermediates in peroxidases, oxygenases and catalases
    • Hersleth HP, Ryde U, Rydberg P, Gorbitz CH, and Andersson KK. Structures of the high-valent metalion haem-oxygen intermediates in peroxidases, oxygenases and catalases. J Inorg Biochem 100: 460-476, 2006.
    • (2006) J Inorg Biochem , vol.100 , pp. 460-476
    • Hersleth, H.P.1    Ryde, U.2    Rydberg, P.3    Gorbitz, C.H.4    Andersson, K.K.5
  • 49
    • 76749094625 scopus 로고    scopus 로고
    • Crystallization of synthetic haemozoin (betahaematin) nucleated at the surface of lipid particles
    • Hoang AN, Ncokazi KK, de Villiers KA, Wright DW, and Egan TJ. Crystallization of synthetic haemozoin (betahaematin) nucleated at the surface of lipid particles. Dalton Trans 39: 1235-1244, 2010.
    • (2010) Dalton Trans , vol.39 , pp. 1235-1244
    • Hoang, A.N.1    Ncokazi, K.K.2    De Villiers, K.A.3    Wright, D.W.4    Egan, T.J.5
  • 50
    • 78649499641 scopus 로고    scopus 로고
    • The neutral lipid composition present in the digestive vacuole of Plasmodium falciparum concentrates heme and mediates beta-hematin formation with an unusually low activation energy
    • Hoang AN, Sandlin RD, Omar A, Egan TJ, and Wright DW. The neutral lipid composition present in the digestive vacuole of Plasmodium falciparum concentrates heme and mediates beta-hematin formation with an unusually low activation energy. Biochemistry 49: 10107-10116, 2010.
    • (2010) Biochemistry , vol.49 , pp. 10107-10116
    • Hoang, A.N.1    Sandlin, R.D.2    Omar, A.3    Egan, T.J.4    Wright, D.W.5
  • 52
    • 0033213013 scopus 로고    scopus 로고
    • The plastid in Plasmodium falciparum asexual blood stages: A three-dimensional ultrastructural analysis
    • Hopkins J, Fowler R, Krishna S, Wilson I, Mitchell G, and Bannister L. The plastid in Plasmodium falciparum asexual blood stages: a three-dimensional ultrastructural analysis. Protist 150: 283-295, 1999. (Pubitemid 29532240)
    • (1999) Protist , vol.150 , Issue.3 , pp. 283-295
    • Hopkins, J.1    Fowler, R.2    Krishna, S.3    Wilson, I.4    Mitchell, G.5    Bannister, L.6
  • 53
    • 0022994181 scopus 로고
    • Secretion of a malarial histidine-rich protein (Pf HRP II) from Plasmodium falciparum-infected erythrocytes
    • DOI 10.1083/jcb.103.4.1269
    • Howard RJ, Uni S, Aikawa M, Aley SB, Leech JH, Lew AM, Wellems TE, Rener J, and Taylor DW. Secretion of a malarial histidine-rich protein (PfHRP II) from Plasmodium falciparum-infected erythrocytes. J Cell Biol 103: 1269-1277, 1986. (Pubitemid 17174153)
    • (1986) Journal of Cell Biology , vol.103 , Issue.4 , pp. 1269-1277
    • Howard, R.J.1    Uni, S.2    Aikawa, M.3
  • 54
    • 79953745644 scopus 로고    scopus 로고
    • The multiple functions of cytochrome c and their regulation in life and death decisions of the mammalian cell: From respiration to apoptosis
    • Huttemann M, Pecina P, Rainbolt M, Sanderson TH, Kagan VE, Samavati L, Doan JW, and Lee I. The multiple functions of cytochrome c and their regulation in life and death decisions of the mammalian cell: from respiration to apoptosis. Mitochondrion 11: 369-381, 2011.
    • (2011) Mitochondrion , vol.11 , pp. 369-381
    • Huttemann, M.1    Pecina, P.2    Rainbolt, M.3    Sanderson, T.H.4    Kagan, V.E.5    Samavati, L.6    Doan, J.W.7    Lee, I.8
  • 55
    • 0006602830 scopus 로고
    • On Porphyria and the Aetiology of Werwolves
    • Illis L. On Porphyria and the Aetiology of Werwolves. Proc R Soc Med 57: 23-26, 1964.
    • (1964) Proc R Soc Med , vol.57 , pp. 23-26
    • Illis, L.1
  • 56
    • 0001164098 scopus 로고
    • Porphyrin Accumulation and Export by Isolated Barley (Hordeum vulgare) Plastids (Effect of Diphenyl Ether Herbicides)
    • Jacobs JM and Jacobs NJ. Porphyrin Accumulation and Export by Isolated Barley (Hordeum vulgare) Plastids (Effect of Diphenyl Ether Herbicides). Plant Physiol 101: 1181-1187, 1993.
    • (1993) Plant Physiol , vol.101 , pp. 1181-1187
    • Jacobs, J.M.1    Jacobs, N.J.2
  • 58
    • 77954636478 scopus 로고    scopus 로고
    • A common red algal origin of the apicomplexan, dinoflagellate, and heterokont plastids
    • Janouskovec J, Horak A, Obornik M, Lukes J, and Keeling PJ. A common red algal origin of the apicomplexan, dinoflagellate, and heterokont plastids. Proc Natl Acad Sci U S A 107: 10949-10954, 2010.
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 10949-10954
    • Janouskovec, J.1    Horak, A.2    Obornik, M.3    Lukes, J.4    Keeling, P.J.5
  • 60
    • 12644261804 scopus 로고
    • The biosynthesis of 5-aminolaevulinic acid and its transformation into uroporphyrinogen III
    • edited by Jordan PM. Amsterdam: Elsevier
    • Jordan PM. The biosynthesis of 5-aminolaevulinic acid and its transformation into uroporphyrinogen III. In: Biosynthesis of Tetrapyrroles, edited by Jordan PM. Amsterdam: Elsevier, 1991, pp. 1-66.
    • (1991) Biosynthesis of Tetrapyrroles , pp. 1-66
    • Jordan, P.M.1
  • 61
    • 78249239490 scopus 로고    scopus 로고
    • Bacterial sulfite-oxidizing enzymes
    • Kappler U. Bacterial sulfite-oxidizing enzymes. Biochim Biophys Acta 1807: 1-10, 2011.
    • (2011) Biochim Biophys Acta , vol.1807 , pp. 1-10
    • Kappler, U.1
  • 64
    • 0001336902 scopus 로고
    • The enzymatic synthesis of delta-aminolevulinic acid
    • Kikuchi G, Kumar A, Talmage P, and Shemin D. The enzymatic synthesis of delta-aminolevulinic acid. J Biol Chem 233: 1214-1219, 1958.
    • (1958) J Biol Chem , vol.233 , pp. 1214-1219
    • Kikuchi, G.1    Kumar, A.2    Talmage, P.3    Shemin, D.4
  • 65
    • 5644247394 scopus 로고    scopus 로고
    • A Plasmodium falciparum dipeptidyl aminopeptidase I participates in vacuolar hemoglobin degradation
    • Klemba M, Gluzman I, and Goldberg DE. A Plasmodium falciparum dipeptidyl aminopeptidase I participates in vacuolar hemoglobin degradation. J Biol Chem 279: 43000- 43007, 2004.
    • (2004) J Biol Chem , vol.279 , pp. 43000-43007
    • Klemba, M.1    Gluzman, I.2    Goldberg, D.E.3
  • 68
    • 74149093650 scopus 로고    scopus 로고
    • Evolution of the haem synthetic pathway in kinetoplastid flagellates: An essential pathway that is not essential after all?
    • Koreny L, Lukes J, and Obornik M. Evolution of the haem synthetic pathway in kinetoplastid flagellates: an essential pathway that is not essential after all? Int J Parasitol 40: 149-156, 2010.
    • (2010) Int J Parasitol , vol.40 , pp. 149-156
    • Koreny, L.1    Lukes, J.2    Obornik, M.3
  • 69
    • 79960105680 scopus 로고    scopus 로고
    • Sequence evidence for the presence of two tetrapyrrole pathways in Euglena gracilis
    • Koreny L and Obornik M. Sequence evidence for the presence of two tetrapyrrole pathways in Euglena gracilis. Genome Biol Evol 3: 359-364, 2011.
    • (2011) Genome Biol Evol , vol.3 , pp. 359-364
    • Koreny, L.1    Obornik, M.2
  • 70
    • 80055012864 scopus 로고    scopus 로고
    • Tetrapyrrole Synthesis of Photosynthetic Chromerids Is Likely Homologous to the Unusual Pathway of Apicomplexan Parasites
    • Koreny L, Sobotka R, Janouskovec J, Keeling PJ, and Obornik M. Tetrapyrrole Synthesis of Photosynthetic Chromerids Is Likely Homologous to the Unusual Pathway of Apicomplexan Parasites. Plant Cell 23: 3454-3462, 2011.
    • (2011) Plant Cell , vol.23 , pp. 3454-3462
    • Koreny, L.1    Sobotka, R.2    Janouskovec, J.3    Keeling, P.J.4    Obornik, M.5
  • 71
    • 0031875674 scopus 로고    scopus 로고
    • Molecular mechanisms of cytochrome c biogenesis: Three distinct systems
    • DOI 10.1046/j.1365-2958.1998.00869.x
    • Kranz R, Lill R, Goldman B, Bonnard G, and Merchant S. Molecular mechanisms of cytochrome c biogenesis: three distinct systems. Mol Microbiol 29: 383-396, 1998. (Pubitemid 28330775)
    • (1998) Molecular Microbiology , vol.29 , Issue.2 , pp. 383-396
    • Kranz, R.1    Lill, R.2    Goldman, B.3    Bonnard, G.4    Merchant, S.5
  • 72
    • 34249740700 scopus 로고    scopus 로고
    • The role of transporters in cellular heme and porphyrin homeostasis
    • DOI 10.1016/j.pharmthera.2007.02.001, PII S016372580700023X
    • Krishnamurthy P, Xie T, and Schuetz JD. The role of transporters in cellular heme and porphyrin homeostasis. Pharmacol Ther 114: 345-358, 2007. (Pubitemid 46843250)
    • (2007) Pharmacology and Therapeutics , vol.114 , Issue.3 , pp. 345-358
    • Krishnamurthy, P.1    Xie, T.2    Schuetz, J.D.3
  • 74
    • 19444386445 scopus 로고    scopus 로고
    • Free heme toxicity and its detoxification systems in human
    • DOI 10.1016/j.toxlet.2005.03.004, PII S0378427405000883
    • Kumar S and Bandyopadhyay U. Free heme toxicity and its detoxification systems in human. Toxicol Lett 157: 175-188, 2005. (Pubitemid 40726102)
    • (2005) Toxicology Letters , vol.157 , Issue.3 , pp. 175-188
    • Kumar, S.1    Bandyopadhyay, U.2
  • 75
    • 0347513216 scopus 로고    scopus 로고
    • Mitochondrial-type iron-sulfur cluster biosynthesis genes (IscS and IscU) in the apicomplexan Cryptosporidium parvum
    • LaGier MJ, Tachezy J, Stejskal F, Kutisova K, and Keithly JS. Mitochondrial-type iron-sulfur cluster biosynthesis genes (IscS and IscU) in the apicomplexan Cryptosporidium parvum. Microbiology 149: 3519-3530, 2003. (Pubitemid 38016679)
    • (2003) Microbiology , vol.149 , Issue.12 , pp. 3519-3530
    • LaGier, M.J.1    Tachezy, J.2    Stejskal, F.3    Kutisova, K.4    Keithly, J.S.5
  • 76
    • 0018230759 scopus 로고
    • Plasmodium falciparum: Merozoite invasion in vitro in the presence of chloroquine
    • Langreth SG, Nguyen-Dinh P, and Trager W. Plasmodium falciparum: merozoite invasion in vitro in the presence of chloroquine. Exp Parasitol 46: 235-238, 1978. (Pubitemid 9090539)
    • (1978) Experimental Parasitology , vol.46 , Issue.2 , pp. 235-238
    • Langreth, S.G.1    Nguyen, D.P.2    Trager, W.3
  • 78
    • 0027405813 scopus 로고
    • Regulation by heme of mitochondrial protein transport through a conserved amino acid motif
    • Lathrop JT and Timko MP. Regulation by heme of mitochondrial protein transport through a conserved amino acid motif. Science 259: 522-525, 1993. (Pubitemid 23058711)
    • (1993) Science , vol.259 , Issue.5094 , pp. 522-525
    • Lathrop, J.T.1    Timko, M.P.2
  • 79
    • 58749104911 scopus 로고    scopus 로고
    • An overview of the Babesia, Plasmodium and Theileria genomes: A comparative perspective
    • Lau AO. An overview of the Babesia, Plasmodium and Theileria genomes: a comparative perspective. Mol Biochem Parasitol 164: 1-8, 2009.
    • (2009) Mol Biochem Parasitol , vol.164 , pp. 1-8
    • Lau, A.O.1
  • 80
    • 20444476656 scopus 로고    scopus 로고
    • Structural divergence and distant relationships in proteins: Evolution of the globins
    • DOI 10.1016/j.sbi.2005.05.008, PII S0959440X05000928
    • Lecomte JT, Vuletich DA, and Lesk AM. Structural divergence and distant relationships in proteins: evolution of the globins. Curr Opin Struct Biol 15: 290-301, 2005. (Pubitemid 40826448)
    • (2005) Current Opinion in Structural Biology , vol.15 , Issue.3 SPEC. ISS. , pp. 290-301
    • Lecomte, J.T.J.1    Vuletich, D.A.2    Lesk, A.M.3
  • 82
    • 80053280973 scopus 로고    scopus 로고
    • Two internal type II NADH dehydrogenases of Toxoplasma gondii are both required for optimal tachyzoite growth
    • Lin SS, Gross U, and Bohne W. Two internal type II NADH dehydrogenases of Toxoplasma gondii are both required for optimal tachyzoite growth. Mol Microbiol 82: 209-221, 2011.
    • (2011) Mol Microbiol , vol.82 , pp. 209-221
    • Lin, S.S.1    Gross, U.2    Bohne, W.3
  • 84
    • 0023932566 scopus 로고
    • Detection of hemin release during hemoglobin S denaturation
    • Liu SC, Zhai S, and Palek J. Detection of hemin release during hemoglobin S denaturation. Blood 71: 1755-1758, 1988.
    • (1988) Blood , vol.71 , pp. 1755-1758
    • Liu, S.C.1    Zhai, S.2    Palek, J.3
  • 85
    • 0018361235 scopus 로고
    • Hemolymph of Anopheles stephensi from noninfected and Plasmodium berghei-infected mosquitoes. 3. Carbohydrates
    • DOI 10.2307/3280149
    • Mack SR, Samuels S, and Vanderberg JP. Hemolymph of Anopheles stephensi from noninfected and Plasmodium berghei-infected mosquitoes. 3. Carbohydrates. J Parasitol 65: 217-221, 1979. (Pubitemid 9239469)
    • (1979) Journal of Parasitology , vol.65 , Issue.2 , pp. 217-221
    • Mack, S.R.1    Samuels, S.2    Vanderberg, J.P.3
  • 86
    • 0014218407 scopus 로고
    • Morphological effects of chloroquine on Plasmodium berghei in mice
    • Macomber PB and Sprinz H. Morphological effects of chloroquine on Plasmodium berghei in mice. Nature 214: 937-939, 1967.
    • (1967) Nature , vol.214 , pp. 937-939
    • Macomber, P.B.1    Sprinz, H.2
  • 87
    • 27544434838 scopus 로고    scopus 로고
    • 30 Some years of heme oxygenase: From a "molecular wrecking ball" to a "mesmerizing" trigger of cellular events
    • DOI 10.1016/j.bbrc.2005.08.121, PII S0006291X05018449
    • Maines MD and Gibbs PE. 30 some years of heme oxygenase: from a "molecular wrecking ball" to a "mesmerizing" trigger of cellular events. Biochem Biophys Res Commun 338: 568-577, 2005. (Pubitemid 41540604)
    • (2005) Biochemical and Biophysical Research Communications , vol.338 , Issue.1 , pp. 568-577
    • Maines, M.D.1    Gibbs, P.E.M.2
  • 89
    • 77956552982 scopus 로고    scopus 로고
    • Regulation of mammalian heme synthesis
    • edited by Warren MJ and Smith AG. Austin: Landes Bioscience
    • Medlock AE and Dailey HA. Regulation of mammalian heme synthesis. In: Tetrapyrroles: Birth, Life and Death, edited by Warren MJ and Smith AG. Austin: Landes Bioscience, 2009, pp. 116-127.
    • (2009) Tetrapyrroles: Birth, Life and Death , pp. 116-127
    • Medlock, A.E.1    Dailey, H.A.2
  • 91
    • 78649251920 scopus 로고    scopus 로고
    • Heme as trigger and target for trioxane-containing antimalarial drugs
    • Meunier B and Robert A. Heme as trigger and target for trioxane-containing antimalarial drugs. Acc Chem Res 43: 1444-1451, 2010.
    • (2010) Acc Chem Res , vol.43 , pp. 1444-1451
    • Meunier, B.1    Robert, A.2
  • 92
    • 0028129356 scopus 로고
    • Malaria pathogenesis
    • Miller LH, Good MF, and Milon G. Malaria pathogenesis. Science 264: 1878-1883, 1994. (Pubitemid 24245626)
    • (1994) Science , vol.264 , Issue.5167 , pp. 1878-1883
    • Miller, L.H.1    Good, M.F.2    Milon, G.3
  • 93
    • 70449094676 scopus 로고    scopus 로고
    • Identification of mitochondrial Complex II subunits SDH3 and SDH4 and ATP synthase subunits a and b in Plasmodium spp
    • Mogi T and Kita K. Identification of mitochondrial Complex II subunits SDH3 and SDH4 and ATP synthase subunits a and b in Plasmodium spp. Mitochondrion 9: 443-453, 2009.
    • (2009) Mitochondrion , vol.9 , pp. 443-453
    • Mogi, T.1    Kita, K.2
  • 95
    • 9644266771 scopus 로고    scopus 로고
    • Defects in the biosynthesis of mitochondrial heme c and heme a in yeast and mammals
    • DOI 10.1016/j.bbabio.2004.09.002, PII S0005272804002671, Euromit 6
    • Moraes CT, Diaz F, and Barrientos A. Defects in the biosynthesis of mitochondrial heme c and heme a in yeast and mammals. Biochim Biophys Acta 1659: 153-159, 2004. (Pubitemid 39575502)
    • (2004) Biochimica et Biophysica Acta - Bioenergetics , vol.1659 , Issue.2-3 , pp. 153-159
    • Moraes, C.T.1    Diaz, F.2    Barrientos, A.3
  • 96
    • 54449096156 scopus 로고    scopus 로고
    • Tetrapyrrole profiling in Arabidopsis seedlings reveals that retrograde plastid nuclear signaling is not due to Mgprotoporphyrin IX accumulation
    • Moulin M, McCormac AC, Terry MJ, and Smith AG. Tetrapyrrole profiling in Arabidopsis seedlings reveals that retrograde plastid nuclear signaling is not due to Mgprotoporphyrin IX accumulation. Proc Natl Acad Sci U S A 105: 15178-15183, 2008.
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 15178-15183
    • Moulin, M.1    McCormac, A.C.2    Terry, M.J.3    Smith, A.G.4
  • 97
    • 59749094634 scopus 로고    scopus 로고
    • Localisation of Plasmodium falciparum uroporphyrinogen III decarboxylase of the hemebiosynthetic pathway in the apicoplast and characterisation of its catalytic properties
    • Nagaraj VA, Arumugam R, Chandra NR, Prasad D, Rangarajan PN, and Padmanaban G. Localisation of Plasmodium falciparum uroporphyrinogen III decarboxylase of the hemebiosynthetic pathway in the apicoplast and characterisation of its catalytic properties. Int J Parasitol 39: 559-568, 2009.
    • (2009) Int J Parasitol , vol.39 , pp. 559-568
    • Nagaraj, V.A.1    Arumugam, R.2    Chandra, N.R.3    Prasad, D.4    Rangarajan, P.N.5    Padmanaban, G.6
  • 99
    • 77955842415 scopus 로고    scopus 로고
    • Protoporphyrinogen IX oxidase from Plasmodium falciparum is anaerobic and is localized to the mitochondrion
    • Nagaraj VA, Arumugam R, Prasad D, Rangarajan PN, and Padmanaban G. Protoporphyrinogen IX oxidase from Plasmodium falciparum is anaerobic and is localized to the mitochondrion. Mol Biochem Parasitol 174: 44-52, 2010.
    • (2010) Mol Biochem Parasitol , vol.174 , pp. 44-52
    • Nagaraj, V.A.1    Arumugam, R.2    Prasad, D.3    Rangarajan, P.N.4    Padmanaban, G.5
  • 100
    • 77951623241 scopus 로고    scopus 로고
    • Characterization of coproporphyrinogen III oxidase in Plasmodium falciparum cytosol
    • Nagaraj VA, Prasad D, Arumugam R, Rangarajan PN, and Padmanaban G. Characterization of coproporphyrinogen III oxidase in Plasmodium falciparum cytosol. Parasitol Int 59: 121-127, 2010.
    • (2010) Parasitol Int , vol.59 , pp. 121-127
    • Nagaraj, V.A.1    Prasad, D.2    Arumugam, R.3    Rangarajan, P.N.4    Padmanaban, G.5
  • 101
    • 68749104332 scopus 로고    scopus 로고
    • Mitochondrial localization of functional ferrochelatase from Plasmodium falciparum
    • Nagaraj VA, Prasad D, Rangarajan PN, and Padmanaban G. Mitochondrial localization of functional ferrochelatase from Plasmodium falciparum. Mol Biochem Parasitol 168: 109-112, 2009.
    • (2009) Mol Biochem Parasitol , vol.168 , pp. 109-112
    • Nagaraj, V.A.1    Prasad, D.2    Rangarajan, P.N.3    Padmanaban, G.4
  • 102
    • 80052339898 scopus 로고    scopus 로고
    • What do human parasites do with a chloroplast anyway?
    • Nair SC and Striepen B. What do human parasites do with a chloroplast anyway? PLoS Biol 9: e1001137, 2011.
    • (2011) PLoS Biol , vol.9
    • Nair, S.C.1    Striepen, B.2
  • 104
    • 73649100238 scopus 로고    scopus 로고
    • Heme-binding protein HRG-1 is induced by insulin-like growth factor I and associates with the vacuolar H+-ATPase to control endosomal pH and receptor trafficking
    • O'Callaghan KM, Ayllon V, O'Keeffe J, Wang Y, Cox OT, Loughran G, Forgac M, and O'Connor R. Heme-binding protein HRG-1 is induced by insulin-like growth factor I and associates with the vacuolar H+-ATPase to control endosomal pH and receptor trafficking. J Biol Chem 285: 381-391, 2010.
    • (2010) J Biol Chem , vol.285 , pp. 381-391
    • O'Callaghan, K.M.1    Ayllon, V.2    O'Keeffe, J.3    Wang, Y.4    Cox, O.T.5    Loughran, G.6    Forgac, M.7    O'Connor, R.8
  • 105
    • 2542640961 scopus 로고    scopus 로고
    • A medicinal chemistry perspective on artemisinin and related endoperoxides
    • DOI 10.1021/jm030571c
    • O'Neill PM and Posner GH. A medicinal chemistry perspective on artemisinin and related endoperoxides. J Med Chem 47: 2945-2964, 2004. (Pubitemid 38702690)
    • (2004) Journal of Medicinal Chemistry , vol.47 , Issue.12 , pp. 2945-2964
    • O'Neill, P.M.1    Posner, G.H.2
  • 106
    • 58149526911 scopus 로고    scopus 로고
    • The novel heme oxygenase-like protein from Plasmodium falciparum converts heme to bilirubin IXalpha in the apicoplast
    • Okada K. The novel heme oxygenase-like protein from Plasmodium falciparum converts heme to bilirubin IXalpha in the apicoplast. FEBS Lett 583: 313-319, 2009.
    • (2009) FEBS Lett , vol.583 , pp. 313-319
    • Okada, K.1
  • 107
    • 0019842424 scopus 로고
    • Hemin lyses malaria parasites
    • Orjih AU, Banyal HS, Chevli R, and Fitch CD. Hemin lyses malaria parasites. Science 214: 667-669, 1981. (Pubitemid 12208587)
    • (1981) Science , vol.214 , Issue.4521 , pp. 667-669
    • Orjih, A.U.1    Banyal, H.S.2    Chevli, R.3    Fitch, C.D.4
  • 108
    • 0021105226 scopus 로고
    • W10BSmL, a mutant of Euglena gracilis var. bacillaris lacking plastids
    • Osafune T and Schiff JA. W10BSmL, a mutant of Euglena gracilis var. bacillaris lacking plastids. Exp Cell Res 148: 530-535, 1983.
    • (1983) Exp Cell Res , vol.148 , pp. 530-535
    • Osafune, T.1    Schiff, J.A.2
  • 109
    • 35348914343 scopus 로고    scopus 로고
    • An alternative model for heme biosynthesis in the malarial parasite
    • DOI 10.1016/j.tibs.2007.09.005, PII S0968000407002150
    • Padmanaban G, Nagaraj VA, and Rangarajan PN. An alternative model for heme biosynthesis in the malarial parasite. Trends Biochem Sci 32: 443-449, 2007. (Pubitemid 47588947)
    • (2007) Trends in Biochemical Sciences , vol.32 , Issue.10 , pp. 443-449
    • Padmanaban, G.1    Nagaraj, V.A.2    Rangarajan, P.N.3
  • 111
    • 33847398001 scopus 로고    scopus 로고
    • Specific role of mitochondrial electron transport in blood-stage Plasmodium falciparum
    • DOI 10.1038/nature05572, PII NATURE05572
    • Painter HJ, Morrisey JM, Mather MW, and Vaidya AB. Specific role of mitochondrial electron transport in bloodstage Plasmodium falciparum. Nature 446: 88-91, 2007. (Pubitemid 46348043)
    • (2007) Nature , vol.446 , Issue.7131 , pp. 88-91
    • Painter, H.J.1    Morrisey, J.M.2    Mather, M.W.3    Vaidya, A.B.4
  • 112
    • 0036667415 scopus 로고    scopus 로고
    • A whole genome view of prokaryotic haem biosynthesis
    • Panek H and O'Brian MR. A whole genome view of prokaryotic haem biosynthesis. Microbiology 148: 2273-2282, 2002.
    • (2002) Microbiology , vol.148 , pp. 2273-2282
    • Panek, H.1    O'Brian, M.R.2
  • 114
    • 1142266269 scopus 로고
    • Pigment Formation and Nuclear Division in Chloroquine-Resistant Malaria Parasites (Plasmodium Berghei, Vincke and Lips, 1948)
    • Peters W. Pigment Formation and Nuclear Division in Chloroquine-Resistant Malaria Parasites (Plasmodium Berghei, Vincke and Lips, 1948). Nature 203: 1290-1291, 1964.
    • (1964) Nature , vol.203 , pp. 1290-1291
    • Peters, W.1
  • 115
    • 0036213690 scopus 로고    scopus 로고
    • Powering mitochondrial protein import
    • DOI 10.1038/nsb0402-234
    • Pfanner N and Truscott KN. Powering mitochondrial protein import. Nat Struct Biol 9: 234-236, 2002. (Pubitemid 34289889)
    • (2002) Nature Structural Biology , vol.9 , Issue.4 , pp. 234-236
    • Pfanner, N.1    Truscott, K.N.2
  • 117
    • 33751244559 scopus 로고    scopus 로고
    • Identification of an Intestinal Folate Transporter and the Molecular Basis for Hereditary Folate Malabsorption
    • DOI 10.1016/j.cell.2006.09.041, PII S009286740601347X
    • Qiu A, Jansen M, Sakaris A, Min SH, Chattopadhyay S, Tsai E, Sandoval C, Zhao R, Akabas MH, and Goldman ID. Identification of an intestinal folate transporter and the molecular basis for hereditary folate malabsorption. Cell 127: 917-928, 2006. (Pubitemid 44792250)
    • (2006) Cell , vol.127 , Issue.5 , pp. 917-928
    • Qiu, A.1    Jansen, M.2    Sakaris, A.3    Min, S.H.4    Chattopadhyay, S.5    Tsai, E.6    Sandoval, C.7    Zhao, R.8    Akabas, M.H.9    Goldman, I.D.10
  • 118
    • 79960991925 scopus 로고    scopus 로고
    • Distribution and biochemical properties of an M1-family aminopeptidase in Plasmodium falciparum indicate a role in vacuolar hemoglobin catabolism
    • Ragheb D, Dalal S, Bompiani KM, Ray WK, and Klemba M. Distribution and biochemical properties of an M1-family aminopeptidase in Plasmodium falciparum indicate a role in vacuolar hemoglobin catabolism. J Biol Chem 286: 27255-27265, 2011.
    • (2011) J Biol Chem , vol.286 , pp. 27255-27265
    • Ragheb, D.1    Dalal, S.2    Bompiani, K.M.3    Ray, W.K.4    Klemba, M.5
  • 123
    • 0344630333 scopus 로고    scopus 로고
    • Cryptosporidium parvum Cpn60 targets a relict organelle
    • DOI 10.1007/s00294-003-0432-1
    • Riordan CE, Ault JG, Langreth SG, and Keithly JS. Cryptosporidium parvum Cpn60 targets a relict organelle. Curr Genet 44: 138-147, 2003. (Pubitemid 37493225)
    • (2003) Current Genetics , vol.44 , Issue.3 , pp. 138-147
    • Riordan, C.E.1    Ault, J.G.2    Langreth, S.G.3    Keithly, J.S.4
  • 126
    • 0028169583 scopus 로고
    • Plasmodium falciparum: The pfmdr2 protein is not overexpressed in chloroquineresistant isolates of the malaria parasite
    • Rubio JP and Cowman AF. Plasmodium falciparum: the pfmdr2 protein is not overexpressed in chloroquineresistant isolates of the malaria parasite. Exp Parasitol 79: 137-147, 1994.
    • (1994) Exp Parasitol , vol.79 , pp. 137-147
    • Rubio, J.P.1    Cowman, A.F.2
  • 127
    • 77952885778 scopus 로고    scopus 로고
    • Succinate dehydrogenase - Assembly, regulation and role in human disease
    • Rutter J, Winge DR, and Schiffman JD. Succinate dehydrogenase - Assembly, regulation and role in human disease. Mitochondrion 10: 393-401, 2010.
    • (2010) Mitochondrion , vol.10 , pp. 393-401
    • Rutter, J.1    Winge, D.R.2    Schiffman, J.D.3
  • 129
    • 1942444611 scopus 로고    scopus 로고
    • Enzymes for heme biosynthesis are found in both the mitochondrion and plastid of the malaria parasite Plasmodium falciparum
    • DOI 10.1078/1434461000169
    • Sato S, Clough B, Coates L, and Wilson RJ. Enzymes for heme biosynthesis are found in both the mitochondrion and plastid of the malaria parasite Plasmodium falciparum. Protist 155: 117-125, 2004. (Pubitemid 38503630)
    • (2004) Protist , vol.155 , Issue.1 , pp. 117-125
    • Sato, S.1    Clough, B.2    Coates, L.3    Wilson, R.J.M.4
  • 130
    • 0036230756 scopus 로고    scopus 로고
    • The genome of Plasmodium falciparum encodes an active delta-aminolevulinic acid dehydratase
    • DOI 10.1007/s00294-002-0273-3
    • Sato S and Wilson RJ. The genome of Plasmodium falciparum encodes an active delta-aminolevulinic acid dehydratase. Curr Genet 40: 391-398, 2002. (Pubitemid 34326621)
    • (2002) Current Genetics , vol.40 , Issue.6 , pp. 391-398
    • Sato, S.1    Wilson, R.J.M.2
  • 131
    • 0037306331 scopus 로고    scopus 로고
    • The many roles of cytochrome b5
    • Schenkman JB and Jansson I. The many roles of cytochrome b5. Pharmacol Ther 97: 139-152, 2003.
    • (2003) Pharmacol Ther , vol.97 , pp. 139-152
    • Schenkman, J.B.1    Jansson, I.2
  • 132
    • 77956256451 scopus 로고    scopus 로고
    • Iron and porphyrin trafficking in heme biogenesis
    • Schultz IJ, Chen C, Paw BH, and Hamza I. Iron and porphyrin trafficking in heme biogenesis. J Biol Chem 285: 26753-26759, 2010.
    • (2010) J Biol Chem , vol.285 , pp. 26753-26759
    • Schultz, I.J.1    Chen, C.2    Paw, B.H.3    Hamza, I.4
  • 133
    • 77954602188 scopus 로고    scopus 로고
    • Plastid-associated porphobilinogen synthase from Toxoplasma gondii: Kinetic and structural properties validate therapeutic potential
    • Shanmugam D, Wu B, Ramirez U, Jaffe EK, and Roos DS. Plastid-associated porphobilinogen synthase from Toxoplasma gondii: kinetic and structural properties validate therapeutic potential. J Biol Chem 285: 22122-22131, 2010.
    • (2010) J Biol Chem , vol.285 , pp. 22122-22131
    • Shanmugam, D.1    Wu, B.2    Ramirez, U.3    Jaffe, E.K.4    Roos, D.S.5
  • 135
    • 0000559527 scopus 로고
    • The utilization of glycine for the synthesis of a porphyrin
    • Shemin D and Rittenberg D. The utilization of glycine for the synthesis of a porphyrin. J Biol Chem 159: 567-568, 1945.
    • (1945) J Biol Chem , vol.159 , pp. 567-568
    • Shemin, D.1    Rittenberg, D.2
  • 136
    • 77958100219 scopus 로고    scopus 로고
    • Innate inflammatory response to the malarial pigment hemozoin
    • Shio MT, Kassa FA, Bellemare MJ, and Olivier M. Innate inflammatory response to the malarial pigment hemozoin. Microbes Infect 12: 889-899, 2010.
    • (2010) Microbes Infect , vol.12 , pp. 889-899
    • Shio, M.T.1    Kassa, F.A.2    Bellemare, M.J.3    Olivier, M.4
  • 137
    • 0022457433 scopus 로고
    • Superoxide dismutase and catalase in Toxoplasma gondii
    • DOI 10.1016/0166-6851(86)90069-1
    • Sibley LD, Lawson R, and Weidner E. Superoxide dismutase and catalase in Toxoplasma gondii. Mol Biochem Parasitol 19: 83-87, 1986. (Pubitemid 16073195)
    • (1986) Molecular and Biochemical Parasitology , vol.19 , Issue.1 , pp. 83-87
    • Sibley, L.D.1    Lawson, R.2    Weidner, E.3
  • 138
    • 0026514177 scopus 로고
    • Inhibition by chloroquine of a novel haem polymerase enzyme activity in malaria trophozoites
    • Slater AF and Cerami A. Inhibition by chloroquine of a novel haem polymerase enzyme activity in malaria trophozoites. Nature 355: 167-169, 1992.
    • (1992) Nature , vol.355 , pp. 167-169
    • Slater, A.F.1    Cerami, A.2
  • 140
    • 0032781364 scopus 로고    scopus 로고
    • Resistance mutations reveal the atovaquone-binding domain of cytochrome b in malaria parasites
    • DOI 10.1046/j.1365-2958.1999.01515.x
    • Srivastava IK, Morrisey JM, Darrouzet E, Daldal F, and Vaidya AB. Resistance mutations reveal the atovaquonebinding domain of cytochrome b in malaria parasites. Mol Microbiol 33: 704-711, 1999. (Pubitemid 29392651)
    • (1999) Molecular Microbiology , vol.33 , Issue.4 , pp. 704-711
    • Srivastava, I.K.1    Morrlsey, J.M.2    Darrouzet, E.3    Daldal, F.4    Vaidya, A.B.5
  • 141
    • 0031052025 scopus 로고    scopus 로고
    • Atovaquone, a broad spectrum antiparasitic drug, collapses mitochondrial membrane potential in a malarial parasite
    • DOI 10.1074/jbc.272.7.3961
    • Srivastava IK, Rottenberg H, and Vaidya AB. Atovaquone, a broad spectrum antiparasitic drug, collapses mitochondrial membrane potential in a malarial parasite. J Biol Chem 272: 3961-3966, 1997. (Pubitemid 27078454)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.7 , pp. 3961-3966
    • Srivastava, I.K.1    Rottenberg, H.2    Vaidya, A.B.3
  • 142
    • 0031948126 scopus 로고    scopus 로고
    • Heme synthesizing enzymes of Plasmodium knowlesi: A simian malarial parasite
    • DOI 10.1006/expr.1998.4193
    • Srivastava P and Pandey VC. Heme synthesizing enzymes of Plasmodium knowlesi: a simian malaria parasite. Exp Parasitol 88: 60-63, 1998. (Pubitemid 28375815)
    • (1998) Experimental Parasitology , vol.88 , Issue.1 , pp. 60-63
    • Srivastava, P.1    Pandey, V.C.2
  • 143
    • 79953660218 scopus 로고    scopus 로고
    • A novel pathway for the biosynthesis of heme in Archaea: Genome-based bioinformatic predictions and experimental evidence
    • Storbeck S, Rolfes S, Raux-Deery E, Warren MJ, Jahn D, and Layer G. A novel pathway for the biosynthesis of heme in Archaea: genome-based bioinformatic predictions and experimental evidence. Archaea 2010: 175050, 2010.
    • (2010) Archaea , vol.2010 , pp. 175050
    • Storbeck, S.1    Rolfes, S.2    Raux-Deery, E.3    Warren, M.J.4    Jahn, D.5    Layer, G.6
  • 144
    • 0347927268 scopus 로고    scopus 로고
    • Chloroplast to nucleus communication triggered by accumulation of Mg-protoporphyrinix
    • DOI 10.1038/nature01204
    • Strand A, Asami T, Alonso J, Ecker JR, and Chory J. Chloroplast to nucleus communication triggered by accumulation of Mg-protoporphyrinIX. Nature 421: 79-83, 2003. (Pubitemid 36077088)
    • (2003) Nature , vol.421 , Issue.6918 , pp. 79-83
    • Strand, A.1    Asami, T.2    Alonso, J.3    Ecker, J.R.4    Chory, J.5
  • 145
    • 0030045312 scopus 로고    scopus 로고
    • Plasmodium hemozoin formation mediated by histidine-rich proteins
    • Sullivan DJ, Jr., Gluzman IY, and Goldberg DE. Plasmodium hemozoin formation mediated by histidine-rich proteins. Science 271: 219-222, 1996.
    • (1996) Science , vol.271 , pp. 219-222
    • Sullivan Jr., D.J.1    Gluzman, I.Y.2    Goldberg, D.E.3
  • 147
    • 0026785410 scopus 로고
    • De novo biosynthesis of heme offers a new chemotherapeutic target in the human malarial parasite
    • Surolia N and Padmanaban G. de novo biosynthesis of heme offers a new chemotherapeutic target in the human malarial parasite. Biochem Biophys Res Commun 187: 744-750, 1992.
    • (1992) Biochem Biophys Res Commun , vol.187 , pp. 744-750
    • Surolia, N.1    Padmanaban, G.2
  • 149
    • 34250807129 scopus 로고    scopus 로고
    • Tetrapyrrole biosynthesis in higher plants
    • DOI 10.1146/annurev.arplant.57.032905.105448
    • Tanaka R and Tanaka A. Tetrapyrrole biosynthesis in higher plants. Annu Rev Plant Biol 58: 321-346, 2007. (Pubitemid 46986328)
    • (2007) Annual Review of Plant Biology , vol.58 , pp. 321-346
    • Tanaka, R.1    Tanaka, A.2
  • 150
    • 84862516590 scopus 로고    scopus 로고
    • Regulation of tetrapyrrole synthesis in higher plants
    • edited by Warren MJ and Smith AG. Austin: Landes Bioscience
    • Terry MJ and Smith AG. Regulation of tetrapyrrole synthesis in higher plants. In: Tetrapyrroles: Birth, Life and Death, edited by Warren MJ and Smith AG. Austin: Landes Bioscience, 2009, pp. 250-262.
    • (2009) Tetrapyrroles: Birth, Life and Death , pp. 250-262
    • Terry, M.J.1    Smith, A.G.2
  • 151
    • 79960659551 scopus 로고    scopus 로고
    • Lon peptidase 1 (LONP1)-dependent breakdown of mitochondrial 5-aminolevulinic acid synthase protein by heme in human liver cells
    • Tian Q, Li T, Hou W, Zheng J, Schrum LW, and Bonkovsky HL. Lon peptidase 1 (LONP1)-dependent breakdown of mitochondrial 5-aminolevulinic acid synthase protein by heme in human liver cells. J Biol Chem 286: 26424-26430, 2011.
    • (2011) J Biol Chem , vol.286 , pp. 26424-26430
    • Tian, Q.1    Li, T.2    Hou, W.3    Zheng, J.4    Schrum, L.W.5    Bonkovsky, H.L.6
  • 152
    • 57649107157 scopus 로고    scopus 로고
    • Bacterial heme-transport proteins and their heme-coordination modes
    • Tong Y and Guo M. Bacterial heme-transport proteins and their heme-coordination modes. Arch Biochem Biophys 481: 1-15, 2009.
    • (2009) Arch Biochem Biophys , vol.481 , pp. 1-15
    • Tong, Y.1    Guo, M.2
  • 156
    • 0034737739 scopus 로고    scopus 로고
    • 2+ transport, and fatty
    • DOI 10.1074/jbc.275.13.9709
    • Uyemura SA, Luo S, Moreno SN, and Docampo R. Oxidative phosphorylation, Ca(2 +) transport, and fatty acidinduced uncoupling in malaria parasites mitochondria. J Biol Chem 275: 9709-9715, 2000. (Pubitemid 30185204)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.13 , pp. 9709-9715
    • Uyemura, S.A.1    Luo, S.2    Moreno, S.N.J.3    Docampo, R.4
  • 157
    • 0347052859 scopus 로고    scopus 로고
    • Oxidative Phosphorylation and Rotenone-insensitive Malate- and NADH-Quinone Oxidoreductases in Plasmodium yoelii yoelii Mitochondria in Situ
    • DOI 10.1074/jbc.M307264200
    • Uyemura SA, Luo S, VieiraM, Moreno SN, and Docampo R. Oxidative phosphorylation and rotenone-insensitive malateand NADH-quinone oxidoreductases in Plasmodium yoelii yoelii mitochondria in situ. J Biol Chem 279: 385-393, 2004. (Pubitemid 38044837)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.1 , pp. 385-393
    • Uyemura, S.A.1    Luo, S.2    Vieira, M.3    Moreno, S.N.J.4    Docampo, R.5
  • 158
    • 78651064576 scopus 로고    scopus 로고
    • The role of cytochrome P450 monooxygenases in microbial fatty acid metabolism
    • Van Bogaert IN, Groeneboer S, Saerens K, and Soetaert W. The role of cytochrome P450 monooxygenases in microbial fatty acid metabolism. FEBS J 278: 206-221, 2011.
    • (2011) FEBS J , vol.278 , pp. 206-221
    • Van Bogaert, I.N.1    Groeneboer, S.2    Saerens, K.3    Soetaert, W.4
  • 159
    • 22144494182 scopus 로고    scopus 로고
    • Development of the endoplasmic reticulum, mitochondrion and apicoplast during the asexual life cycle of Plasmodium falciparum
    • DOI 10.1111/j.1365-2958.2005.04699.x
    • van Dooren GG, Marti M, Tonkin CJ, Stimmler LM, Cowman AF, and McFadden GI. Development of the endoplasmic reticulum, mitochondrion and apicoplast during the asexual life cycle of Plasmodium falciparum. Mol Microbiol 57: 405-419, 2005. (Pubitemid 40979342)
    • (2005) Molecular Microbiology , vol.57 , Issue.2 , pp. 405-419
    • Van Dooren, G.G.1    Marti, M.2    Tonkin, C.J.3    Stimmler, L.M.4    Cowman, A.F.5    McFadden, G.I.6
  • 160
    • 33744956145 scopus 로고    scopus 로고
    • Metabolic maps and functions of the Plasmodium mitochondrion
    • DOI 10.1111/j.1574-6976.2006.00027.x
    • van Dooren GG, Stimmler LM, and McFadden GI. Metabolic maps and functions of the Plasmodium mitochondrion. FEMS Microbiol Rev 30: 596-630, 2006. (Pubitemid 43855768)
    • (2006) FEMS Microbiology Reviews , vol.30 , Issue.4 , pp. 596-630
    • Van Dooren, G.G.1    Stimmler, L.M.2    McFadden, G.I.3
  • 161
    • 0022653719 scopus 로고
    • Characterization of a hemoglobin-degrading, low molecular weight protease from Plasmodium falciparum
    • DOI 10.1016/0166-6851(86)90095-2
    • Vander Jagt DL, Hunsaker LA, and Campos NM. Characterization of a hemoglobin-degrading, low molecular weight protease from Plasmodium falciparum. Mol Biochem Parasitol 18: 389-400, 1986. (Pubitemid 16158493)
    • (1986) Molecular and Biochemical Parasitology , vol.18 , Issue.3 , pp. 389-400
    • Vander, J.D.L.1    Hunsaker, L.A.2    Campos, N.M.3
  • 162
    • 43249131048 scopus 로고    scopus 로고
    • A haptoglobin-hemoglobin receptor conveys innate immunity to Trypanosoma brucei in humans
    • DOI 10.1126/science.1156296
    • Vanhollebeke B, De Muylder G, Nielsen MJ, Pays A, Tebabi P, Dieu M, Raes M, Moestrup SK, and Pays E. A haptoglobin-hemoglobin receptor conveys innate immunity to Trypanosoma brucei in humans. Science 320: 677-681, 2008. (Pubitemid 351928352)
    • (2008) Science , vol.320 , Issue.5876 , pp. 677-681
    • Vanhollebeke, B.1    De Muylder, G.2    Nielsen, M.J.3    Pays, A.4    Tebabi, P.5    Dieu, M.6    Raes, M.7    Moestrup, S.K.8    Pays, E.9
  • 163
    • 0037108901 scopus 로고    scopus 로고
    • Involvement of delta-aminolaevulinate synthase encoded by the parasite gene in de novo haem synthesis by Plasmodium falciparum
    • DOI 10.1042/BJ20020834
    • Varadharajan S,Dhanasekaran S, Bonday ZQ, Rangarajan PN, and Padmanaban G. Involvement of delta-aminolaevulinate synthase encoded by the parasite gene in de novo haem synthesis by Plasmodium falciparum. Biochem J 367: 321-327, 2002. (Pubitemid 35216806)
    • (2002) Biochemical Journal , vol.367 , Issue.2 , pp. 321-327
    • Varadharajan, S.1    Dhanasekaran, S.2    Bonday, Z.Q.3    Rangarajan, P.N.4    Padmanaban, G.5
  • 165
    • 0032553547 scopus 로고    scopus 로고
    • Respiration and oxidative phosphorylation in the apicomplexan parasite Toxoplasma gondii
    • DOI 10.1074/jbc.273.47.31040
    • Vercesi AE, Rodrigues CO, Uyemura SA, Zhong L, and Moreno SN. Respiration and oxidative phosphorylation in the apicomplexan parasite Toxoplasma gondii. J Biol Chem 273: 31040-31047, 1998. (Pubitemid 28533110)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.47 , pp. 31040-31047
    • Vercesi, A.E.1    Rodrigues, C.O.2    Uyemura, S.A.3    Zhong, L.4    Moreno, S.N.J.5
  • 166
    • 84862573160 scopus 로고    scopus 로고
    • Tetrapyrroles in photodynaminc therapy
    • edited by Warren MJ and Smith AG. Austin: Landes Bioscience
    • Vernon DI and Walker I. Tetrapyrroles in photodynaminc therapy. In: Tetrapyrroles: Birth, Life and Death, edited by Warren MJ and Smith AG. Austin: Landes Bioscience, 2009, pp. 128-148.
    • (2009) Tetrapyrroles: Birth, Life and Death , pp. 128-148
    • Vernon, D.I.1    Walker, I.2
  • 167
    • 44049108195 scopus 로고    scopus 로고
    • Diversity of globin function: Enzymatic, transport, storage, and sensing
    • Vinogradov SN and Moens L. Diversity of globin function: enzymatic, transport, storage, and sensing. J Biol Chem 283: 8773-8777, 2008.
    • (2008) J Biol Chem , vol.283 , pp. 8773-8777
    • Vinogradov, S.N.1    Moens, L.2
  • 168
    • 77957895003 scopus 로고    scopus 로고
    • The transforming parasite Theileria co-opts host cell mitotic and central spindles to persist in continuously dividing cells
    • von Schubert C, Xue G, Schmuckli-Maurer J, Woods KL, Nigg EA, and Dobbelaere DA. The transforming parasite Theileria co-opts host cell mitotic and central spindles to persist in continuously dividing cells. PLoS Biol 8: e1000499, 2010.
    • (2010) PLoS Biol , vol.8
    • Von Schubert, C.1    Xue, G.2    Schmuckli-Maurer, J.3    Woods, K.L.4    Nigg, E.A.5    Dobbelaere, D.A.6
  • 169
    • 77949661216 scopus 로고    scopus 로고
    • Artemisinin directly targets malarial mitochondria through its specific mitochondrial activation
    • Wang J, Huang L, Li J, Fan Q, Long Y, Li Y, and Zhou B. Artemisinin directly targets malarial mitochondria through its specific mitochondrial activation. PLoS One 5: e9582, 2010.
    • (2010) PLoS One , vol.5
    • Wang, J.1    Huang, L.2    Li, J.3    Fan, Q.4    Long, Y.5    Li, Y.6    Zhou, B.7
  • 170
    • 0014218449 scopus 로고
    • Mode of action of chloroquine on Plasmodium berghei and P. cynomolgi
    • Warhurst DC and Hockley DJ. Mode of action of chloroquine on Plasmodium berghei and P. cynomolgi. Nature 214: 935-936, 1967.
    • (1967) Nature , vol.214 , pp. 935-936
    • Warhurst, D.C.1    Hockley, D.J.2
  • 171
    • 0021099519 scopus 로고
    • Separate physiological roles and subcellular compartments for two tetrapyrrole biosynthetic pathways in Euglena gracilis
    • Weinstein JD and Beale SI. Separate physiological roles and subcellular compartments for two tetrapyrrole biosynthetic pathways in Euglena gracilis. J Biol Chem 258: 6799-6807, 1983.
    • (1983) J Biol Chem , vol.258 , pp. 6799-6807
    • Weinstein, J.D.1    Beale, S.I.2
  • 172
    • 0030179502 scopus 로고    scopus 로고
    • Characterization of the delta-aminolevulinate synthase gene homologue in P. falciparum
    • Wilson CM, SmithAB, and Baylon RV. Characterization of the delta-aminolevulinate synthase gene homologue in P. falciparum. Mol Biochem Parasitol 79: 135-140, 1996.
    • (1996) Mol Biochem Parasitol , vol.79 , pp. 135-140
    • Wilson, C.M.1    Smith, A.B.2    Baylon, R.V.3
  • 174
    • 79957526624 scopus 로고    scopus 로고
    • Heme synthesis by plastid ferrochelatase I regulates nuclear gene expression in plants
    • Woodson JD, Perez-Ruiz JM, and Chory J. Heme synthesis by plastid ferrochelatase I regulates nuclear gene expression in plants. Curr Biol 21: 897-903, 2011.
    • (2011) Curr Biol , vol.21 , pp. 897-903
    • Woodson, J.D.1    Perez-Ruiz, J.M.2    Chory, J.3
  • 176
    • 80052308799 scopus 로고    scopus 로고
    • Chemical rescue of malaria parasites lacking an apicoplast defines organelle function in bloodstage Plasmodium falciparum
    • Yeh E and DeRisi JL. Chemical rescue of malaria parasites lacking an apicoplast defines organelle function in bloodstage Plasmodium falciparum. PLoS Biol 9: e1001138, 2011.
    • (2011) PLoS Biol , vol.9
    • Yeh, E.1    DeRisi, J.L.2
  • 180
    • 77954309588 scopus 로고    scopus 로고
    • Evolution of structure and function of Class I peroxidases
    • Zamocky M, Furtmuller PG, and Obinger C. Evolution of structure and function of Class I peroxidases. Arch Biochem Biophys 500: 45-57, 2010.
    • (2010) Arch Biochem Biophys , vol.500 , pp. 45-57
    • Zamocky, M.1    Furtmuller, P.G.2    Obinger, C.3
  • 181
    • 33750065106 scopus 로고    scopus 로고
    • Evaluating the roles of the heme a side chains in cytochrome c oxidase using designed heme proteins
    • DOI 10.1021/bi060565t
    • Zhuang J, Reddi AR, Wang Z, Khodaverdian B, Hegg EL, and Gibney BR. Evaluating the roles of the heme a side chains in cytochrome c oxidase using designed heme proteins. Biochemistry 45: 12530-12538, 2006. (Pubitemid 44583695)
    • (2006) Biochemistry , vol.45 , Issue.41 , pp. 12530-12538
    • Zhuang, J.1    Reddi, A.R.2    Wang, Z.3    Khodaverdian, B.4    Hegg, E.L.5    Gibney, B.R.6


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