메뉴 건너뛰기




Volumn 3, Issue 12, 2007, Pages 1938-1949

Apicoplast lipoic acid protein ligase B is not essential for Plasmodium falciparum

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA KETO ACID DEHYDROGENASE; ENZYME; GLYCINE; LIGASE; LIPB ENZYME; LPLA2 ENZYME; OXIDOREDUCTASE; PYRUVATE DEHYDROGENASE; THIOCTIC ACID; UNCLASSIFIED DRUG; LIPOATE PROTEIN LIGASE; LIPOATE-PROTEIN LIGASE; LIPOPROTEIN; PEPTIDE SYNTHASE; PROTOZOAL DNA; PROTOZOAL PROTEIN;

EID: 37849040526     PISSN: 15537366     EISSN: 15537374     Source Type: Journal    
DOI: 10.1371/journal.ppat.0030189     Document Type: Article
Times cited : (46)

References (53)
  • 1
    • 0033790516 scopus 로고    scopus 로고
    • Swinging arms and swinging domains in multifunctional enzymes: Catalytic machines for multistep reactions
    • Perham RN (2000) Swinging arms and swinging domains in multifunctional enzymes: catalytic machines for multistep reactions. Annu Rev Biochem 69: 961-1004.
    • (2000) Annu Rev Biochem , vol.69 , pp. 961-1004
    • Perham, R.N.1
  • 4
    • 0034953587 scopus 로고    scopus 로고
    • Lipoic acid metabolism in Arabidopsis thaliana: Cloning and characterization of a cDNA encoding lipoyltransferase
    • Wada M, Yasuno R, Jordan SW, Cronan JE Jr, Wada H (2001) Lipoic acid metabolism in Arabidopsis thaliana: cloning and characterization of a cDNA encoding lipoyltransferase. Plant Cell. Physiol 42: 650-656.
    • (2001) Plant Cell. Physiol , vol.42 , pp. 650-656
    • Wada, M.1    Yasuno, R.2    Jordan, S.W.3    Cronan Jr, J.E.4    Wada, H.5
  • 5
    • 0037165633 scopus 로고    scopus 로고
    • The biosynthetic pathway for lipoic acid is present in plastids and mitochondria in Arabidopsis thaliana
    • Yasuno R, Wada H (2002) The biosynthetic pathway for lipoic acid is present in plastids and mitochondria in Arabidopsis thaliana. FEBS Lett 517: 110-114.
    • (2002) FEBS Lett , vol.517 , pp. 110-114
    • Yasuno, R.1    Wada, H.2
  • 6
    • 26444504579 scopus 로고    scopus 로고
    • Function, attachment and synthesis of lipoic acid in Escherichia coli
    • Cronan JE, Zhao X, Jiang Y (2005) Function, attachment and synthesis of lipoic acid in Escherichia coli. Adv Microb Physiol 50: 103-146.
    • (2005) Adv Microb Physiol , vol.50 , pp. 103-146
    • Cronan, J.E.1    Zhao, X.2    Jiang, Y.3
  • 7
    • 0348229020 scopus 로고    scopus 로고
    • Assembly of the covalent linkage between lipoic acid and its cognate enzymes
    • Zhao X, Miller JR, Jiang Y, Marletta MA, Cronan JE (2003) Assembly of the covalent linkage between lipoic acid and its cognate enzymes. Chem Biol 10, 1293-1302.
    • (2003) Chem Biol , vol.10 , pp. 1293-1302
    • Zhao, X.1    Miller, J.R.2    Jiang, Y.3    Marletta, M.A.4    Cronan, J.E.5
  • 8
    • 29244461444 scopus 로고    scopus 로고
    • The reaction of LipB, the octanoyl-[acyl carrier protein]:protein N-octanoyltransferase of lipoic acid synthesis, proceeds through an acyl-enzyme intermediate
    • Zhao X, Miller JR, Cronan JE (2005) The reaction of LipB, the octanoyl-[acyl carrier protein]:protein N-octanoyltransferase of lipoic acid synthesis, proceeds through an acyl-enzyme intermediate. Biochemistry 44: 16737-16746.
    • (2005) Biochemistry , vol.44 , pp. 16737-16746
    • Zhao, X.1    Miller, J.R.2    Cronan, J.E.3
  • 9
    • 0028244665 scopus 로고
    • Purification and characterization of lipoyl-AMP:N epsilon-lysine lipoyltransferase from bovine liver mitochondria
    • Fujiwara K, Okamura-Ikeda K, Motokawa Y (1994) Purification and characterization of lipoyl-AMP:N epsilon-lysine lipoyltransferase from bovine liver mitochondria. J Biol Chem 269: 16605-16609.
    • (1994) J Biol Chem , vol.269 , pp. 16605-16609
    • Fujiwara, K.1    Okamura-Ikeda, K.2    Motokawa, Y.3
  • 10
    • 0035800735 scopus 로고    scopus 로고
    • Purification, characterization, and cDNA cloning of lipoate-activating enzyme from bovine liver
    • Fujiwara K, Takeuchi S, Okamura-Ikeda K, Motokawa Y (2001) Purification, characterization, and cDNA cloning of lipoate-activating enzyme from bovine liver. J Biol Chem 276: 28819-28823.
    • (2001) J Biol Chem , vol.276 , pp. 28819-28823
    • Fujiwara, K.1    Takeuchi, S.2    Okamura-Ikeda, K.3    Motokawa, Y.4
  • 11
    • 0038304827 scopus 로고    scopus 로고
    • Apicomplexan parasites contain a single lipoic acid synthase located in the plastid
    • Thomsen-Zieger N, Schachtner J, Seeber F (2003) Apicomplexan parasites contain a single lipoic acid synthase located in the plastid. FEBS Lett 547: 80-86.
    • (2003) FEBS Lett , vol.547 , pp. 80-86
    • Thomsen-Zieger, N.1    Schachtner, J.2    Seeber, F.3
  • 12
    • 3142630285 scopus 로고    scopus 로고
    • The human malaria parasite Plasmodium falciparum has distinct organelle-specific lipoylation pathways
    • Wrenger C, Müller S (2004) The human malaria parasite Plasmodium falciparum has distinct organelle-specific lipoylation pathways. Mol Microbiol 53: 103-113.
    • (2004) Mol Microbiol , vol.53 , pp. 103-113
    • Wrenger, C.1    Müller, S.2
  • 13
    • 33746284201 scopus 로고    scopus 로고
    • Toxoplasma gondii scavenges host-derived lipoic acid despite its de novo synthesis in the apicoplast
    • Crawford MJ, Thomsen-Zieger N, Ray M, Schachtner J, Roos DS, et al. (2006) Toxoplasma gondii scavenges host-derived lipoic acid despite its de novo synthesis in the apicoplast. EMBO J 25: 3214-3222.
    • (2006) EMBO J , vol.25 , pp. 3214-3222
    • Crawford, M.J.1    Thomsen-Zieger, N.2    Ray, M.3    Schachtner, J.4    Roos, D.S.5
  • 14
    • 33846965950 scopus 로고    scopus 로고
    • Scavenging of the cofactor lipoate is essential for the survival of the malaria parasite Plasmodium falciparum
    • Allary M, Lu JZ, Zhu L, Prigge ST (2007) Scavenging of the cofactor lipoate is essential for the survival of the malaria parasite Plasmodium falciparum. Mol Microbiol 63: 1331-1344.
    • (2007) Mol Microbiol , vol.63 , pp. 1331-1344
    • Allary, M.1    Lu, J.Z.2    Zhu, L.3    Prigge, S.T.4
  • 15
    • 33748353213 scopus 로고    scopus 로고
    • Mazumdar J, H Wilson E, Masek K, A Hunter C, Striepen B (2006) Apicoplast fatty acid synthesis is essential for organelle biogenesis and parasite survival in Toxoplasma gondii. Proc Natl Acad Sci U S A 103: 13192-13197.
    • Mazumdar J, H Wilson E, Masek K, A Hunter C, Striepen B (2006) Apicoplast fatty acid synthesis is essential for organelle biogenesis and parasite survival in Toxoplasma gondii. Proc Natl Acad Sci U S A 103: 13192-13197.
  • 16
    • 12344312032 scopus 로고    scopus 로고
    • The malaria parasite Plasmodium falciparum has only one pyruvate dehydrogenase complex, which is located in the apicoplast
    • Foth BJ, Stimmler LM, Handman E, Crabb BS, Hodder AN, et al. (2005) The malaria parasite Plasmodium falciparum has only one pyruvate dehydrogenase complex, which is located in the apicoplast. Mol Microbiol 55: 39-53.
    • (2005) Mol Microbiol , vol.55 , pp. 39-53
    • Foth, B.J.1    Stimmler, L.M.2    Handman, E.3    Crabb, B.S.4    Hodder, A.N.5
  • 17
    • 12344298301 scopus 로고    scopus 로고
    • The human malaria parasite Plasmodium falciparum possesses two distinct dihydrolipoamide dehydrogenases
    • McMillan PJ, Stimmler LM, Foth BJ, McFadden GI, Müller S (2005) The human malaria parasite Plasmodium falciparum possesses two distinct dihydrolipoamide dehydrogenases. Mol Microbiol 55: 27-38.
    • (2005) Mol Microbiol , vol.55 , pp. 27-38
    • McMillan, P.J.1    Stimmler, L.M.2    Foth, B.J.3    McFadden, G.I.4    Müller, S.5
  • 18
    • 27844559736 scopus 로고    scopus 로고
    • Plasmodium falciparum possesses organelle-specific alpha-keto acid dehydrogenase complexes and lipoylation pathways
    • Günther S, McMillan PJ, Wallace LJ, Müller S (2005) Plasmodium falciparum possesses organelle-specific alpha-keto acid dehydrogenase complexes and lipoylation pathways. Biochem Soc Trans 33: 977-980.
    • (2005) Biochem Soc Trans , vol.33 , pp. 977-980
    • Günther, S.1    McMillan, P.J.2    Wallace, L.J.3    Müller, S.4
  • 19
    • 0034708162 scopus 로고    scopus 로고
    • Pgh1 modulates sensitivity and resistance to multiple antimalarials in Plasmodium falciparum
    • Reed MB, Saliba KJ, Caruana SR, Kirk K, Cowman AF (2000) Pgh1 modulates sensitivity and resistance to multiple antimalarials in Plasmodium falciparum. Nature 403: 906-909.
    • (2000) Nature , vol.403 , pp. 906-909
    • Reed, M.B.1    Saliba, K.J.2    Caruana, S.R.3    Kirk, K.4    Cowman, A.F.5
  • 20
    • 33745011804 scopus 로고    scopus 로고
    • The Mycobacterium tuberculosis LipB enzyme functions as a cysteine/lysine dyad acyltransferase
    • Ma Q, Zhao X, Nasser Eddine A, Geerlof A, Li X, et al. (2006) The Mycobacterium tuberculosis LipB enzyme functions as a cysteine/lysine dyad acyltransferase. Proc Natl Acad Sci USA 103: 8662-8667.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 8662-8667
    • Ma, Q.1    Zhao, X.2    Nasser Eddine, A.3    Geerlof, A.4    Li, X.5
  • 21
    • 33745630355 scopus 로고    scopus 로고
    • A set of glycosylphosphatidyl inositol-anchored membrane proteins of Plasmodium falciparum is refractory to genetic deletion
    • Sanders PR, Kats LM, Drew DR, O'Donnell RA, O'Neill M, et al. (2006) A set of glycosylphosphatidyl inositol-anchored membrane proteins of Plasmodium falciparum is refractory to genetic deletion. Infect Immun 74: 4330-4338.
    • (2006) Infect Immun , vol.74 , pp. 4330-4338
    • Sanders, P.R.1    Kats, L.M.2    Drew, D.R.3    O'Donnell, R.A.4    O'Neill, M.5
  • 22
    • 33845987535 scopus 로고    scopus 로고
    • Fatty acid biosynthesis as a drug target in apicomplexan parasites
    • Goodman CD, McFadden GI (2007) Fatty acid biosynthesis as a drug target in apicomplexan parasites. Curr Drug Targets 8: 15-30.
    • (2007) Curr Drug Targets , vol.8 , pp. 15-30
    • Goodman, C.D.1    McFadden, G.I.2
  • 23
    • 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 (2001) Triclosan offers protection against blood stages of malaria by inhibiting enoyl-ACP reductase of Plasmodium falciparum. Nat Med 7: 167-173.
    • (2001) Nat Med , vol.7 , pp. 167-173
    • Surolia, N.1    Surolia, A.2
  • 24
    • 0027401765 scopus 로고
    • Lipoic acid metabolism in Escherichia coli: Sequencing and functional characterization of the lipA and lipB genes
    • Reed KE, Cronan JE Jr (1993) Lipoic acid metabolism in Escherichia coli: sequencing and functional characterization of the lipA and lipB genes. J Bacteriol 175: 1325-1336.
    • (1993) J Bacteriol , vol.175 , pp. 1325-1336
    • Reed, K.E.1    Cronan Jr, J.E.2
  • 25
    • 0028821293 scopus 로고
    • Lipoic acid metabolism in Escherichia coli: The lplA and lipB genes define redundant pathways for ligation of lipoyl groups to apoprotein
    • Morris TW, Reed KE, Cronan JE Jr (1995) Lipoic acid metabolism in Escherichia coli: the lplA and lipB genes define redundant pathways for ligation of lipoyl groups to apoprotein. J Bacteriol 177: 1-10.
    • (1995) J Bacteriol , vol.177 , pp. 1-10
    • Morris, T.W.1    Reed, K.E.2    Cronan Jr, J.E.3
  • 26
    • 0036777601 scopus 로고    scopus 로고
    • Chromosomal amplification of the Escherichia coli lipB region confers high-level resistance to selenolipoic acid
    • Jordan SW, Cronan JE Jr (2002) Chromosomal amplification of the Escherichia coli lipB region confers high-level resistance to selenolipoic acid. J Bacteriol 184: 5495-5501.
    • (2002) J Bacteriol , vol.184 , pp. 5495-5501
    • Jordan, S.W.1    Cronan Jr, J.E.2
  • 27
    • 25844453475 scopus 로고    scopus 로고
    • Crystal structure of lipoate-protein ligase A from Escherichia coli. Determination of the lipoic acid-binding site
    • Fujiwara K, Toma S, Okamura-Ikeda K, Motokawa Y, Nakagawa A, et al. (2005) Crystal structure of lipoate-protein ligase A from Escherichia coli. Determination of the lipoic acid-binding site. J Biol Chem 280: 33645-33651.
    • (2005) J Biol Chem , vol.280 , pp. 33645-33651
    • Fujiwara, K.1    Toma, S.2    Okamura-Ikeda, K.3    Motokawa, Y.4    Nakagawa, A.5
  • 28
    • 27844503528 scopus 로고    scopus 로고
    • Crystal structure of lipoate-protein ligase A bound with the activated intermediate: Insights into interaction with lipoyl domains
    • Kim DJ, Kim KH, Lee HH, Lee SJ, Ha JY, et al. (2005) Crystal structure of lipoate-protein ligase A bound with the activated intermediate: insights into interaction with lipoyl domains. J Biol Chem 280: 38081-38089.
    • (2005) J Biol Chem , vol.280 , pp. 38081-38089
    • Kim, D.J.1    Kim, K.H.2    Lee, H.H.3    Lee, S.J.4    Ha, J.Y.5
  • 29
    • 31344446409 scopus 로고    scopus 로고
    • Structure of a putative lipoate protein ligase from Thermoplasma acidophilum and the mechanism of target selection for post-translational modification
    • McManus E, Luisi BF, Perham RN (2006) Structure of a putative lipoate protein ligase from Thermoplasma acidophilum and the mechanism of target selection for post-translational modification. J Mol Biol 356: 625-637.
    • (2006) J Mol Biol , vol.356 , pp. 625-637
    • McManus, E.1    Luisi, B.F.2    Perham, R.N.3
  • 30
    • 0345073644 scopus 로고    scopus 로고
    • Protein farnesyl and N-myristoyl transferases: Piggy-back medicinal chemistry targets for the development of antitrypanosomatid and antimalarial therapeutics
    • Gelb MH, Van Voorhis WC, Buckner FS, Yokoyama K, Eastman R, et al. (2003) Protein farnesyl and N-myristoyl transferases: piggy-back medicinal chemistry targets for the development of antitrypanosomatid and antimalarial therapeutics. Mol Biochem Parasitol 126: 155-163.
    • (2003) Mol Biochem Parasitol , vol.126 , pp. 155-163
    • Gelb, M.H.1    Van Voorhis, W.C.2    Buckner, F.S.3    Yokoyama, K.4    Eastman, R.5
  • 32
    • 0036070514 scopus 로고    scopus 로고
    • Antioxidant and prooxidant activities of alpha-lipoic acid and dihydrolipoic acid
    • Moini H, Packer L, Saris NE (2002) Antioxidant and prooxidant activities of alpha-lipoic acid and dihydrolipoic acid. Toxicol Appl Pharmacol 182: 84-90.
    • (2002) Toxicol Appl Pharmacol , vol.182 , pp. 84-90
    • Moini, H.1    Packer, L.2    Saris, N.E.3
  • 33
    • 0024459019 scopus 로고
    • Reductive acetylation of tandemly repeated lipoyl domains in the pyruvate dehydrogenase multienzyme complex of Escherichia coli is random order
    • Allen AG, Perham RN, Allison N, Miles JS, Guest JR (1989) Reductive acetylation of tandemly repeated lipoyl domains in the pyruvate dehydrogenase multienzyme complex of Escherichia coli is random order. J Mol Biol 208: 623-633.
    • (1989) J Mol Biol , vol.208 , pp. 623-633
    • Allen, A.G.1    Perham, R.N.2    Allison, N.3    Miles, J.S.4    Guest, J.R.5
  • 34
    • 0141733057 scopus 로고    scopus 로고
    • Plasmodium falciparum falcilysin: A metalloprotease with dual specificity
    • Murata CE, Goldberg DE (2003) Plasmodium falciparum falcilysin: a metalloprotease with dual specificity. J Biol Chem 278: 38022-38028.
    • (2003) J Biol Chem , vol.278 , pp. 38022-38028
    • Murata, C.E.1    Goldberg, D.E.2
  • 35
    • 33846039237 scopus 로고    scopus 로고
    • Subcellular multitasking - multiple destinations and roles for the Plasmodium falcilysin protease
    • Ralph SA (2007) Subcellular multitasking - multiple destinations and roles for the Plasmodium falcilysin protease. Mol Microbiol 63: 309-313.
    • (2007) Mol Microbiol , vol.63 , pp. 309-313
    • Ralph, S.A.1
  • 36
    • 25844434373 scopus 로고    scopus 로고
    • Plant organellar protein targeting: A traffic plan still under construction
    • Mackenzie SA (2005) Plant organellar protein targeting: a traffic plan still under construction. Trends Cell Biol 15: 548-554.
    • (2005) Trends Cell Biol , vol.15 , pp. 548-554
    • Mackenzie, S.A.1
  • 37
    • 33749624260 scopus 로고    scopus 로고
    • Recent surprises in protein targeting to mitochondria and plastids
    • Millar AH, Whelan J, Small I (2006) Recent surprises in protein targeting to mitochondria and plastids. Curr Opin Plant Biol 9: 610-615.
    • (2006) Curr Opin Plant Biol , vol.9 , pp. 610-615
    • Millar, A.H.1    Whelan, J.2    Small, I.3
  • 38
    • 33644649331 scopus 로고    scopus 로고
    • Combining experimental and predicted datasets for determination of the subcellular location of proteins in Arabidopsis
    • Heazlewood JL, Tonti-Filippini J, Verboom RE, Millar AH (2005) Combining experimental and predicted datasets for determination of the subcellular location of proteins in Arabidopsis. Plant Physiol 139: 598-609.
    • (2005) Plant Physiol , vol.139 , pp. 598-609
    • Heazlewood, J.L.1    Tonti-Filippini, J.2    Verboom, R.E.3    Millar, A.H.4
  • 39
    • 33644876148 scopus 로고    scopus 로고
    • Dual-domain, dual-targeting organellar protein presequences in Arabidopsis can use non-AUG start codons
    • Christensen AC, Lyznik A, Mohammed S, Elowsky CG, Elo A, et al. (2005) Dual-domain, dual-targeting organellar protein presequences in Arabidopsis can use non-AUG start codons. Plant Cell 17: 2805-2816.
    • (2005) Plant Cell , vol.17 , pp. 2805-2816
    • Christensen, A.C.1    Lyznik, A.2    Mohammed, S.3    Elowsky, C.G.4    Elo, A.5
  • 40
    • 33746284200 scopus 로고    scopus 로고
    • Protein targeting to destinations of the secretory pathway in the malaria parasite Plasmodium falciparum
    • Tonkin CJ, Pearce JA, McFadden GI, Cowman AF (2006) Protein targeting to destinations of the secretory pathway in the malaria parasite Plasmodium falciparum. Curr Opin Microbiol 9: 381-387.
    • (2006) Curr Opin Microbiol , vol.9 , pp. 381-387
    • Tonkin, C.J.1    Pearce, J.A.2    McFadden, G.I.3    Cowman, A.F.4
  • 41
    • 34548440314 scopus 로고    scopus 로고
    • Dual targeting of antioxidant and metabolic enzymes to the mitochondrion and the apicoplast of Toxoplasma gondii
    • Pino P, Foth BJ, Kwok LY, Sheiner L, Schepers R, et al. (2007) Dual targeting of antioxidant and metabolic enzymes to the mitochondrion and the apicoplast of Toxoplasma gondii. PLoS Pathog 3: 115-132.
    • (2007) PLoS Pathog , vol.3 , pp. 115-132
    • Pino, P.1    Foth, B.J.2    Kwok, L.Y.3    Sheiner, L.4    Schepers, R.5
  • 42
    • 0017311840 scopus 로고
    • Human malaria parasites in continuous culture
    • Trager W, Jensen JB (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
  • 43
    • 0018704491 scopus 로고
    • Synchronization of Plasmodium falciparum erythrocytic stages in culture
    • Lambros C, Vanderberg JP (1979) Synchronization of Plasmodium falciparum erythrocytic stages in culture. J Parasitol 65: 418-420.
    • (1979) J Parasitol , vol.65 , pp. 418-420
    • Lambros, C.1    Vanderberg, J.P.2
  • 44
    • 0030006717 scopus 로고    scopus 로고
    • Characterization of promoters and stable transfection by homologous and nonhomologous recombination in Plasmodium falciparum
    • Crabb BS, Cowman AF (1996) Characterization of promoters and stable transfection by homologous and nonhomologous recombination in Plasmodium falciparum. Proc Natl Acad Sci USA 93: 7289-7294.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 7289-7294
    • Crabb, B.S.1    Cowman, A.F.2
  • 45
    • 0030035041 scopus 로고    scopus 로고
    • Transformation of Plasmodium falciparum malaria parasites by homologous integration of plasmids that confer resistance to pyrimethamine
    • Wu Y, Kirkman LA, Wellems TE (1996) Transformation of Plasmodium falciparum malaria parasites by homologous integration of plasmids that confer resistance to pyrimethamine. Proc Natl Acad Sci USA 93: 1130-1134.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 1130-1134
    • Wu, Y.1    Kirkman, L.A.2    Wellems, T.E.3
  • 46
    • 0030176163 scopus 로고    scopus 로고
    • Plasmodium falciparum: Isolation of large numbers of parasite clones from infected blood samples
    • Kirkman LA, Su XZ, Wellems TE (1996) Plasmodium falciparum: isolation of large numbers of parasite clones from infected blood samples. Exp Parasitol 83: 147-149.
    • (1996) Exp Parasitol , vol.83 , pp. 147-149
    • Kirkman, L.A.1    Su, X.Z.2    Wellems, T.E.3
  • 47
    • 0032407858 scopus 로고    scopus 로고
    • Cycloguanil and its parent compound proguanil demonstrate distinct activities against Plasmodium falciparum malaria parasites transformed with human dihydrofolate reductase
    • Fidock DA, Nomura T, Wellems TE (1998) Cycloguanil and its parent compound proguanil demonstrate distinct activities against Plasmodium falciparum malaria parasites transformed with human dihydrofolate reductase. Mol Pharmacol 54: 1140-1147.
    • (1998) Mol Pharmacol , vol.54 , pp. 1140-1147
    • Fidock, D.A.1    Nomura, T.2    Wellems, T.E.3
  • 48
    • 0015089766 scopus 로고
    • New thick-film technique for malaria diagnosis. Use of saponin stromatolytic solution for lysis
    • Umlas J, Fallon JN (1971) New thick-film technique for malaria diagnosis. Use of saponin stromatolytic solution for lysis. Am Med Trop Med Hyg 20: 527-529.
    • (1971) Am Med Trop Med Hyg , vol.20 , pp. 527-529
    • Umlas, J.1    Fallon, J.N.2
  • 49
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72: 248-254.
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 51
    • 0024510418 scopus 로고
    • Detection of bacterial lipoic acid. A modified gas-chromatographic-mass-spectrometric procedure
    • Pratt KJ, Carles C, Carne TJ, Danson MJ, Stevenson KJ (1989) Detection of bacterial lipoic acid. A modified gas-chromatographic-mass-spectrometric procedure. Biochem J 258: 749-754.
    • (1989) Biochem J , vol.258 , pp. 749-754
    • Pratt, K.J.1    Carles, C.2    Carne, T.J.3    Danson, M.J.4    Stevenson, K.J.5
  • 52
    • 22144494182 scopus 로고    scopus 로고
    • Development of the endoplasmic reticulum, mitochondrion and apicoplast during the asexual life cycle of Plasmodium falciparum
    • van Dooren GG, Marti M, Tonkin CJ, Stimmler LM, Cowman AF, et al. (2005) Development of the endoplasmic reticulum, mitochondrion and apicoplast during the asexual life cycle of Plasmodium falciparum. Mol Microbiol 57: 405-419.
    • (2005) Mol Microbiol , vol.57 , pp. 405-419
    • van Dooren, G.G.1    Marti, M.2    Tonkin, C.J.3    Stimmler, L.M.4    Cowman, A.F.5
  • 53
    • 3343010591 scopus 로고    scopus 로고
    • Localization of organellar proteins in Plasmodium falciparum using a novel set of transfection vectors and a new immunofluorescence fixation method
    • Tonkin CJ, van Dooren GG, Spurck TP, Struck NS, Good RT, et al. (2004) Localization of organellar proteins in Plasmodium falciparum using a novel set of transfection vectors and a new immunofluorescence fixation method. Mol Biochem Parasitol 137: 13-21.
    • (2004) Mol Biochem Parasitol , vol.137 , pp. 13-21
    • Tonkin, C.J.1    van Dooren, G.G.2    Spurck, T.P.3    Struck, N.S.4    Good, R.T.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.