메뉴 건너뛰기




Volumn 384, Issue 2, 2004, Pages 429-436

Localization of ferrochelatase in Plasmodium falciparum

Author keywords

Apicoplast; Ferrochelatase; Haem synthesis; Localization; Mitochondrion; Plasmodium falciparum

Indexed keywords

ANTIBODIES; BIODIVERSITY; BIOSYNTHESIS; CYTOLOGY; ENZYME KINETICS; GENES;

EID: 10644227681     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20040952     Document Type: Article
Times cited : (45)

References (31)
  • 1
    • 0026785410 scopus 로고
    • De novo biosynthesis of haem offers a new chemotherapeutic target in the human malarial parasite
    • Surolia, N. and Padmanaban, G. (1992) De novo biosynthesis of haem offers a new chemotherapeutic target in the human malarial parasite. Biochem. Biophys. Res. Commun. 187, 744-750
    • (1992) Biochem. Biophys. Res. Commun. , vol.187 , pp. 744-750
    • Surolia, N.1    Padmanaban, G.2
  • 2
    • 0030758361 scopus 로고    scopus 로고
    • Haem biosynthesis by the malarial parasite - Import of δ-aminolaevulinate dehydratase from the host red cell
    • Bonday, Z. Q., Taketani, S., Gupta, P. D. and Padmanaban, G. (1997) Haem biosynthesis by the malarial parasite - import of δ-aminolaevulinate dehydratase from the host red cell. J. Biol. Chem. 272, 21839-21846
    • (1997) J. Biol. Chem. , vol.272 , pp. 21839-21846
    • Bonday, Z.Q.1    Taketani, S.2    Gupta, P.D.3    Padmanaban, G.4
  • 3
    • 0029670146 scopus 로고    scopus 로고
    • Characterization of the δ-aminalaevulinate synthase gene homologue from P. falciparum
    • Wilson, C. M., Smith, A. B. and Baylon, R. V. (1996) Characterization of the δ-aminalaevulinate synthase gene homologue from P. falciparum. Mol. Biochem. Parasitol. 75, 271-276
    • (1996) Mol. Biochem. Parasitol. , vol.75 , pp. 271-276
    • Wilson, C.M.1    Smith, A.B.2    Baylon, R.V.3
  • 4
    • 0037108901 scopus 로고    scopus 로고
    • Involvement of δ-aminolaevulinate synthase encoded by the parasite gene in de novo haem synthesis by Plasmodium falciparum
    • Varadharajan, S., Dhanasekaran, S., Rangarajan, P. N. and Padmanaban, G. (2002) Involvement of δ-aminolaevulinate synthase encoded by the parasite gene in de novo haem synthesis by Plasmodium falciparum. Biochem. J. 367, 321-327
    • (2002) Biochem. J. , vol.367 , pp. 321-327
    • Varadharajan, S.1    Dhanasekaran, S.2    Rangarajan, P.N.3    Padmanaban, G.4
  • 5
    • 0033834719 scopus 로고    scopus 로고
    • Import of host delta-aminolaevulinate dehydratase into the malarial parasite. Identification of a new drug target
    • Bonday, Z. Q., Dhanasekaran, S., Rangarajan, P. N. and Padmanaban, G. (2000) Import of host delta-aminolaevulinate dehydratase into the malarial parasite. Identification of a new drug target. Nat. Med. 6, 898-903
    • (2000) Nat. Med , vol.6 , pp. 898-903
    • Bonday, Z.Q.1    Dhanasekaran, S.2    Rangarajan, P.N.3    Padmanaban, G.4
  • 7
    • 0036230756 scopus 로고    scopus 로고
    • The genome of Plasmodium falciparum encodes an active δ-aminolaevulinic acid dehydratase
    • Sato, S. and Wilson, R. J. M. (2002) The genome of Plasmodium falciparum encodes an active δ-aminolaevulinic acid dehydratase. Curr. Genet. 40, 391-398
    • (2002) Curr. Genet. , vol.40 , pp. 391-398
    • Sato, S.1    Wilson, R.J.M.2
  • 8
    • 0034114697 scopus 로고    scopus 로고
    • Impact of a plastid bearing endosymbiont on apicomplexan genomes
    • Sato, S., Tews, I. and Wilson, R. J. M. (2000) Impact of a plastid bearing endosymbiont on apicomplexan genomes. Int. J. Parasitol. 30, 427-439
    • (2000) Int. J. Parasitol. , vol.30 , pp. 427-439
    • Sato, S.1    Tews, I.2    Wilson, R.J.M.3
  • 9
    • 1342325384 scopus 로고    scopus 로고
    • δ-aminolaevulinic acid dehydratase from Plasmodium falciparum - Indigenous vs imported
    • Dhanasekaran, S., Chandra, N. R., Sagar, B. K. C., Rangarajan, P. N. and Padmanaban, G. (2004) δ-Aminolaevulinic acid dehydratase from Plasmodium falciparum - indigenous vs imported. J. Biol. Chem. 279, 6934-6942
    • (2004) J. Biol. Chem. , vol.279 , pp. 6934-6942
    • Dhanasekaran, S.1    Chandra, N.R.2    Sagar, B.K.C.3    Rangarajan, P.N.4    Padmanaban, G.5
  • 10
    • 0022425318 scopus 로고
    • Orientation of ferrochelatase in bovine liver mitochondria
    • Harbin, B. M. and Dailey, H. A. (1985) Orientation of ferrochelatase in bovine liver mitochondria. Biochemistry 24, 366-370
    • (1985) Biochemistry , vol.24 , pp. 366-370
    • Harbin, B.M.1    Dailey, H.A.2
  • 11
    • 0000624972 scopus 로고    scopus 로고
    • Two different genes encode ferrochelatase in Arabidopsis: Mapping, expression and cellular targeting of the precursor proteins
    • Chow, J. S., Singh, D. P., Walker, A. R. and Smith, A. G. (1998) Two different genes encode ferrochelatase in Arabidopsis: mapping, expression and cellular targeting of the precursor proteins. Plant J. 15, 531-541
    • (1998) Plant J. , vol.15 , pp. 531-541
    • Chow, J.S.1    Singh, D.P.2    Walker, A.R.3    Smith, A.G.4
  • 12
    • 0042853494 scopus 로고    scopus 로고
    • Subcellular localization of two types of ferrochelatase in cucumber
    • Masuda, T., Suzuki, T., Shimada, H., Ohta, H. and Takaniya, K. (2003) Subcellular localization of two types of ferrochelatase in cucumber. Planta 217, 602-609
    • (2003) Planta , vol.217 , pp. 602-609
    • Masuda, T.1    Suzuki, T.2    Shimada, H.3    Ohta, H.4    Takaniya, K.5
  • 13
    • 0037295433 scopus 로고    scopus 로고
    • Proteobacteria-like ferrochelatase in the malaria parasite
    • Sato, S. and Wilson, R. J. M. (2003) Proteobacteria-like ferrochelatase in the malaria parasite. Curr. Genet. 42, 292-300
    • (2003) Curr. Genet. , vol.42 , pp. 292-300
    • Sato, S.1    Wilson, R.J.M.2
  • 15
    • 0024483266 scopus 로고
    • Fluorescent labeling of mitochondria
    • Chen, L. B. (1989) Fluorescent labeling of mitochondria. Methods Cell Biol. 30, 103-123
    • (1989) Methods Cell Biol. , vol.30 , pp. 103-123
    • Chen, L.B.1
  • 16
    • 0017311840 scopus 로고
    • Human malaria parasites in continuous culture
    • Trager, W. and Jensen, J. B. (1976) Human malaria parasites in continuous culture. Science 193, 673-675
    • (1976) Science , vol.193 , pp. 673-675
    • Trager, W.1    Jensen, J.B.2
  • 18
    • 1342314457 scopus 로고
    • Preparation of crude fractions from host-parasite complex
    • (Panyim, S., Wilairat, P. and Yuthawong, Y., eds.), Mahidol University, Bangkok
    • Sirawaraporn, W. (1985) Preparation of crude fractions from host-parasite complex. In Genetic Engineering Techniques in Tropical Diseases Research (Panyim, S., Wilairat, P. and Yuthawong, Y., eds.), pp. 407-412, Mahidol University, Bangkok
    • (1985) Genetic Engineering Techniques in Tropical Diseases Research , pp. 407-412
    • Sirawaraporn, W.1
  • 19
    • 0022559009 scopus 로고
    • Purification and characterization of mammalian and chicken ferrochelatase
    • Dailey, H. A., Fleming, J. E. and Harbin, B. E. (1986) Purification and characterization of mammalian and chicken ferrochelatase. Methods Enzymol. 123, 401-408
    • (1986) Methods Enzymol. , vol.123 , pp. 401-408
    • Dailey, H.A.1    Fleming, J.E.2    Harbin, B.E.3
  • 20
  • 21
    • 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. (1999) The plastid in Plasmodium falciparum asexual blood stages: a three dimensional ultrastructural analysis. Protist 150, 283-295
    • (1999) Protist , vol.150 , pp. 283-295
    • Hopkins, J.1    Fowler, R.2    Krishna, S.3    Wilson, I.4    Mitchell, G.5    Bannister, L.6
  • 22
    • 0035798637 scopus 로고    scopus 로고
    • Localization of the Plasmodium falciparum PfNT nucleoside transporter to the parasite plasma membrane
    • Rager, N., Ben Mamoun, C., Carter, N. S., Goldberg, D. E. and Ullman, B. (2001) Localization of the Plasmodium falciparum PfNT nucleoside transporter to the parasite plasma membrane. J. Biol. Chem. 276, 41095-41099
    • (2001) J. Biol. Chem. , vol.276 , pp. 41095-41099
    • Rager, N.1    Ben Mamoun, C.2    Carter, N.S.3    Goldberg, D.E.4    Ullman, B.5
  • 23
    • 0032080066 scopus 로고    scopus 로고
    • Identification and characterization of an unusual double serine/threonine protein phosphatase 2C in the malarial parasite Plasmodium falciparum
    • Ben Mamoun, C., Sullivan, D. J., Banerjee, R. and Goldberg, D. E. (1998) Identification and characterization of an unusual double serine/threonine protein phosphatase 2C in the malarial parasite Plasmodium falciparum. J. Biol. Chem. 273, 11241-11247
    • (1998) J. Biol. Chem. , vol.273 , pp. 11241-11247
    • Ben Mamoun, C.1    Sullivan, D.J.2    Banerjee, R.3    Goldberg, D.E.4
  • 24
    • 0035951353 scopus 로고    scopus 로고
    • Inhibition of 15-lipoxygenase leads to delayed organelle degradation in the reticulocyte
    • Grullich, C., Duvoisin, R. M., Wiedmann, M. and van Leyden, K. (2001) Inhibition of 15-lipoxygenase leads to delayed organelle degradation in the reticulocyte. FEBS Lett. 489, 51-54
    • (2001) FEBS Lett. , vol.489 , pp. 51-54
    • Grullich, C.1    Duvoisin, R.M.2    Wiedmann, M.3    Van Leyden, K.4
  • 25
    • 0021977242 scopus 로고
    • Autophagy of mitochondria in rat bone marrow erythroid cells. Relation to nuclear extrusion
    • Heynen, M. J., Tricot, G. and Verwilghen, R. L. (1985) Autophagy of mitochondria in rat bone marrow erythroid cells. Relation to nuclear extrusion. Cell Tissue Res. 239, 235-239
    • (1985) Cell Tissue Res. , vol.239 , pp. 235-239
    • Heynen, M.J.1    Tricot, G.2    Verwilghen, R.L.3
  • 26
    • 0016780261 scopus 로고
    • A lipoxygenase in rabbit reticulocytes which attacks phospholipids and intact mitochondria
    • Schewe, T., Halangk, W., Hiebsch, C. and Papoport, S. M. (1975) A lipoxygenase in rabbit reticulocytes which attacks phospholipids and intact mitochondria. FEBS Lett. 60, 149-152
    • (1975) FEBS Lett. , vol.60 , pp. 149-152
    • Schewe, T.1    Halangk, W.2    Hiebsch, C.3    Papoport, S.M.4
  • 27
    • 0034678922 scopus 로고    scopus 로고
    • Protein targeting to the plastid of Plasmodium falciparum is via the secretory pathway
    • Waller, R. F., Reed, M. B., Cowman, A. F. and McFadden, G. I. (2000) Protein targeting to the plastid of Plasmodium falciparum is via the secretory pathway. EMBO J. 19, 1794-1802
    • (2000) EMBO J. , vol.19 , pp. 1794-1802
    • Waller, R.F.1    Reed, M.B.2    Cowman, A.F.3    McFadden, G.I.4
  • 30
    • 0002132016 scopus 로고
    • Biosynthesis of 5-aminolevulinic acid and its transformation into coporphyrinogen in animals and bacteria
    • (Dailey, H. A., ed.), McGraw-Hill, New York
    • Jordan, P. N. (1990) Biosynthesis of 5-aminolevulinic acid and its transformation into coporphyrinogen in animals and bacteria. In Biosynthesis of Haem and Chlorophyll (Dailey, H. A., ed.), pp. 55-121, McGraw-Hill, New York
    • (1990) Biosynthesis of Haem and Chlorophyll , pp. 55-121
    • Jordan, P.N.1
  • 31
    • 0034794448 scopus 로고    scopus 로고
    • Regulatory network of tetrapyrrole biosynthesis-studies of intracellular signalling involved in metabolic and developmental control of plastids
    • Papenbrock, J. and Grimm, B. (2001) Regulatory network of tetrapyrrole biosynthesis-studies of intracellular signalling involved in metabolic and developmental control of plastids. Planta 213, 667-681
    • (2001) Planta , vol.213 , pp. 667-681
    • Papenbrock, J.1    Grimm, B.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.