메뉴 건너뛰기




Volumn 8, Issue 3, 2013, Pages

Loss of pH Control in Plasmodium falciparum Parasites Subjected to Oxidative Stress

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; HYDROGEN PEROXIDE; INORGANIC PYROPHOSPHATASE;

EID: 84874918957     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0058933     Document Type: Article
Times cited : (25)

References (58)
  • 2
    • 0015502066 scopus 로고
    • The generation of superoxide radical during the autoxidation of hemoglobin
    • Misra HP, Fridovich I, (1972) The generation of superoxide radical during the autoxidation of hemoglobin. J Biol Chem 247: 6960-6962.
    • (1972) J Biol Chem , vol.247 , pp. 6960-6962
    • Misra, H.P.1    Fridovich, I.2
  • 3
    • 0027430639 scopus 로고
    • Origin of reactive oxygen species in erythrocytes infected with Plasmodium falciparum
    • Atamna H, Ginsburg H, (1993) Origin of reactive oxygen species in erythrocytes infected with Plasmodium falciparum. Mol Biochem Parasitol 61: 231-241.
    • (1993) Mol Biochem Parasitol , vol.61 , pp. 231-241
    • Atamna, H.1    Ginsburg, H.2
  • 4
    • 0021342123 scopus 로고
    • Killing of Plasmodium yoelii by enzyme-induced products of the oxidative burst
    • Dockrell HM, Playfair JH, (1984) Killing of Plasmodium yoelii by enzyme-induced products of the oxidative burst. Infect Immun 43: 451-456.
    • (1984) Infect Immun , vol.43 , pp. 451-456
    • Dockrell, H.M.1    Playfair, J.H.2
  • 6
    • 1242316941 scopus 로고    scopus 로고
    • Oxidative stress in malaria parasite-infected erythrocytes: host-parasite interactions
    • Becker K, Tilley L, Vennerstrom JL, Roberts D, Rogerson S, et al. (2004) Oxidative stress in malaria parasite-infected erythrocytes: host-parasite interactions. Int J Parasitol 34: 163-189.
    • (2004) Int J Parasitol , vol.34 , pp. 163-189
    • Becker, K.1    Tilley, L.2    Vennerstrom, J.L.3    Roberts, D.4    Rogerson, S.5
  • 7
    • 36149001369 scopus 로고    scopus 로고
    • Peroxiredoxins in malaria parasites: parasitologic aspects
    • Kawazu S, Komaki-Yasuda K, Oku H, Kano S, (2008) Peroxiredoxins in malaria parasites: parasitologic aspects. Parasitol Int 57: 1-7.
    • (2008) Parasitol Int , vol.57 , pp. 1-7
    • Kawazu, S.1    Komaki-Yasuda, K.2    Oku, H.3    Kano, S.4
  • 8
    • 69449106780 scopus 로고    scopus 로고
    • The malarial parasite Plasmodium falciparum imports the human protein peroxiredoxin 2 for peroxide detoxification
    • Koncarevic S, Rohrbach P, Deponte M, Krohne G, Prieto JH, et al. (2009) The malarial parasite Plasmodium falciparum imports the human protein peroxiredoxin 2 for peroxide detoxification. Proc Natl Acad Sci USA 106: 13323-13328.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 13323-13328
    • Koncarevic, S.1    Rohrbach, P.2    Deponte, M.3    Krohne, G.4    Prieto, J.H.5
  • 9
    • 0020672571 scopus 로고
    • Killing of blood-stage murine malaria parasites by hydrogen peroxide
    • Dockrell HM, Playfair JH, (1983) Killing of blood-stage murine malaria parasites by hydrogen peroxide. Infect Immun 39: 456-459.
    • (1983) Infect Immun , vol.39 , pp. 456-459
    • Dockrell, H.M.1    Playfair, J.H.2
  • 10
    • 0020696254 scopus 로고
    • Evidence for reactive oxygen intermediates causing hemolysis and parasite death in malaria
    • Clark IA, Hunt NH, (1983) Evidence for reactive oxygen intermediates causing hemolysis and parasite death in malaria. Infect Immun 39: 1-6.
    • (1983) Infect Immun , vol.39 , pp. 1-6
    • Clark, I.A.1    Hunt, N.H.2
  • 11
    • 0021267950 scopus 로고
    • Activity of divicine in Plasmodium vinckei-infected mice has implications for treatment of favism and epidemiology of G-6-PD deficiency
    • Clark IA, Cowden WB, Hunt NH, Maxwell LE, Mackie EJ, (1984) Activity of divicine in Plasmodium vinckei-infected mice has implications for treatment of favism and epidemiology of G-6-PD deficiency. Br J Haematol 57: 479-487.
    • (1984) Br J Haematol , vol.57 , pp. 479-487
    • Clark, I.A.1    Cowden, W.B.2    Hunt, N.H.3    Maxwell, L.E.4    Mackie, E.J.5
  • 12
    • 0021183548 scopus 로고
    • Radical-mediated damage to parasites and erythrocytes in Plasmodium vinckei infected mice after injection of t-butyl hydroperoxide
    • Clark IA, Hunt NH, Cowden WB, Maxwell LE, Mackie EJ, (1984) Radical-mediated damage to parasites and erythrocytes in Plasmodium vinckei infected mice after injection of t-butyl hydroperoxide. Clin Exp Immunol 56: 524-530.
    • (1984) Clin Exp Immunol , vol.56 , pp. 524-530
    • Clark, I.A.1    Hunt, N.H.2    Cowden, W.B.3    Maxwell, L.E.4    Mackie, E.J.5
  • 13
    • 0023622465 scopus 로고
    • The antimalarial action on Plasmodium falciparum of qinghaosu and artesunate in combination with agents which modulate oxidant stress
    • Krungkrai SR, Yuthavong Y, (1987) The antimalarial action on Plasmodium falciparum of qinghaosu and artesunate in combination with agents which modulate oxidant stress. Trans R Soc Trop Med Hyg 81: 710-714.
    • (1987) Trans R Soc Trop Med Hyg , vol.81 , pp. 710-714
    • Krungkrai, S.R.1    Yuthavong, Y.2
  • 14
    • 79960992639 scopus 로고    scopus 로고
    • Artemisinin activity against Plasmodium falciparum requires hemoglobin uptake and digestion
    • Klonis N, Crespo-Ortiz MP, Bottova I, Abu-Bakar N, Kenny S, et al. (2011) Artemisinin activity against Plasmodium falciparum requires hemoglobin uptake and digestion. Proc Natl Acad Sci USA 108: 11405-11410.
    • (2011) Proc Natl Acad Sci USA , vol.108 , pp. 11405-11410
    • Klonis, N.1    Crespo-Ortiz, M.P.2    Bottova, I.3    Abu-Bakar, N.4    Kenny, S.5
  • 15
    • 84867087846 scopus 로고    scopus 로고
    • Mechanisms of in vitro resistance to dihydroartemisinin in Plasmodium falciparum
    • Cui L, Wang Z, Miao J, Miao M, Chandra R, et al. (2012) Mechanisms of in vitro resistance to dihydroartemisinin in Plasmodium falciparum. Mol Microbiol 86: 111-128.
    • (2012) Mol Microbiol , vol.86 , pp. 111-128
    • Cui, L.1    Wang, Z.2    Miao, J.3    Miao, M.4    Chandra, R.5
  • 16
    • 43849112193 scopus 로고    scopus 로고
    • Chloroquine mediates specific proteome oxidative damage across the erythrocytic cycle of resistant Plasmodium falciparum
    • Radfar A, Diez A, Bautista JM, (2008) Chloroquine mediates specific proteome oxidative damage across the erythrocytic cycle of resistant Plasmodium falciparum. Free Radic Biol Med 44: 2034-2042.
    • (2008) Free Radic Biol Med , vol.44 , pp. 2034-2042
    • Radfar, A.1    Diez, A.2    Bautista, J.M.3
  • 18
    • 0022503788 scopus 로고
    • Damage to malaria-infected erythrocytes following exposure to oxidant-generating systems
    • Wozencraft AO, (1986) Damage to malaria-infected erythrocytes following exposure to oxidant-generating systems. Parasitology 92: 559-567.
    • (1986) Parasitology , vol.92 , pp. 559-567
    • Wozencraft, A.O.1
  • 19
    • 0037020172 scopus 로고    scopus 로고
    • Illumination of the malaria parasite Plasmodium falciparum alters intracellular pH. Implications for live cell imaging
    • Wissing F, Sanchez CP, Rohrbach P, Ricken S, Lanzer M, (2002) Illumination of the malaria parasite Plasmodium falciparum alters intracellular pH. Implications for live cell imaging. J Biol Chem 277: 37747-37755.
    • (2002) J Biol Chem , vol.277 , pp. 37747-37755
    • Wissing, F.1    Sanchez, C.P.2    Rohrbach, P.3    Ricken, S.4    Lanzer, M.5
  • 20
    • 35748956775 scopus 로고    scopus 로고
    • Evaluation of pH during cytostomal endocytosis and vacuolar catabolism of haemoglobin in Plasmodium falciparum
    • Klonis N, Tan O, Jackson K, Goldberg D, Klemba M, et al. (2007) Evaluation of pH during cytostomal endocytosis and vacuolar catabolism of haemoglobin in Plasmodium falciparum. Biochem J 407: 343-354.
    • (2007) Biochem J , vol.407 , pp. 343-354
    • Klonis, N.1    Tan, O.2    Jackson, K.3    Goldberg, D.4    Klemba, M.5
  • 21
    • 71549139434 scopus 로고    scopus 로고
    • Plasmodium falciparum culture: The benefits of shaking
    • Allen RJ, Kirk K, (2010) Plasmodium falciparum culture: The benefits of shaking. Mol Biochem Parasitol 169: 63-65.
    • (2010) Mol Biochem Parasitol , vol.169 , pp. 63-65
    • Allen, R.J.1    Kirk, K.2
  • 22
    • 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
  • 23
    • 0037458576 scopus 로고    scopus 로고
    • Acidification of the malaria parasite's digestive vacuole by a H+-ATPase and a H+-pyrophosphatase
    • Saliba KJ, Allen RJ, Zissis S, Bray PG, Ward SA, et al. (2003) Acidification of the malaria parasite's digestive vacuole by a H+-ATPase and a H+-pyrophosphatase. J Biol Chem 278: 5605-5612.
    • (2003) J Biol Chem , vol.278 , pp. 5605-5612
    • Saliba, K.J.1    Allen, R.J.2    Zissis, S.3    Bray, P.G.4    Ward, S.A.5
  • 24
    • 52049119746 scopus 로고    scopus 로고
    • Acid extrusion from the intraerythrocytic malaria parasite is not via a Na+/H+ exchanger
    • Spillman NJ, Allen RJ, Kirk K, (2008) Acid extrusion from the intraerythrocytic malaria parasite is not via a Na+/H+ exchanger. Mol Biochem Parasitol 162: 96-99.
    • (2008) Mol Biochem Parasitol , vol.162 , pp. 96-99
    • Spillman, N.J.1    Allen, R.J.2    Kirk, K.3
  • 25
    • 0033584993 scopus 로고    scopus 로고
    • pH regulation in the intracellular malaria parasite, Plasmodium falciparum. H+ extrusion via a V-type H+-ATPase
    • Saliba KJ, Kirk K, (1999) pH regulation in the intracellular malaria parasite, Plasmodium falciparum. H+ extrusion via a V-type H+-ATPase. J Biol Chem 274: 33213-33219.
    • (1999) J Biol Chem , vol.274 , pp. 33213-33219
    • Saliba, K.J.1    Kirk, K.2
  • 26
    • 0022347074 scopus 로고
    • Antimalarials increase vesicle pH in Plasmodium falciparum
    • Krogstad DJ, Schlesinger PH, Gluzman IY, (1985) Antimalarials increase vesicle pH in Plasmodium falciparum. J Cell Biol 101: 2302-2309.
    • (1985) J Cell Biol , vol.101 , pp. 2302-2309
    • Krogstad, D.J.1    Schlesinger, P.H.2    Gluzman, I.Y.3
  • 27
    • 46249086673 scopus 로고    scopus 로고
    • A verapamil-sensitive chloroquine-associated H+ leak from the digestive vacuole in chloroquine-resistant malaria parasites
    • Lehane AM, Hayward R, Saliba KJ, Kirk K, (2008) A verapamil-sensitive chloroquine-associated H+ leak from the digestive vacuole in chloroquine-resistant malaria parasites. J Cell Sci 121: 1624-1632.
    • (2008) J Cell Sci , vol.121 , pp. 1624-1632
    • Lehane, A.M.1    Hayward, R.2    Saliba, K.J.3    Kirk, K.4
  • 28
    • 54349125693 scopus 로고    scopus 로고
    • The inhibitory effect of 2-halo derivatives of D-glucose on glycolysis and on the proliferation of the human malaria parasite Plasmodium falciparum
    • van Schalkwyk DA, Priebe W, Saliba KJ, (2008) The inhibitory effect of 2-halo derivatives of D-glucose on glycolysis and on the proliferation of the human malaria parasite Plasmodium falciparum. J Pharmacol Exp Ther 327: 511-517.
    • (2008) J Pharmacol Exp Ther , vol.327 , pp. 511-517
    • van Schalkwyk, D.A.1    Priebe, W.2    Saliba, K.J.3
  • 29
    • 0032562763 scopus 로고    scopus 로고
    • Transport and metabolism of the essential vitamin pantothenic acid in human erythrocytes infected with the malaria parasite Plasmodium falciparum
    • Saliba KJ, Horner HA, Kirk K, (1998) Transport and metabolism of the essential vitamin pantothenic acid in human erythrocytes infected with the malaria parasite Plasmodium falciparum. J Biol Chem 273: 10190-10195.
    • (1998) J Biol Chem , vol.273 , pp. 10190-10195
    • Saliba, K.J.1    Horner, H.A.2    Kirk, K.3
  • 30
    • 84870003252 scopus 로고    scopus 로고
    • Glutathione export from human erythrocytes and Plasmodium falciparum malaria parasites
    • Barrand MA, Winterberg M, Ng F, Nguyen M, Kirk K, et al. (2012) Glutathione export from human erythrocytes and Plasmodium falciparum malaria parasites. Biochem J 448: 389-400.
    • (2012) Biochem J , vol.448 , pp. 389-400
    • Barrand, M.A.1    Winterberg, M.2    Ng, F.3    Nguyen, M.4    Kirk, K.5
  • 31
    • 0034602263 scopus 로고    scopus 로고
    • Vacuolar H+-ATPase localized in plasma membranes of malaria parasite cells, Plasmodium falciparum, is involved in regional acidification of parasitized erythrocytes
    • Hayashi M, Yamada H, Mitamura T, Horii T, Yamamoto A, et al. (2000) Vacuolar H+-ATPase localized in plasma membranes of malaria parasite cells, Plasmodium falciparum, is involved in regional acidification of parasitized erythrocytes. J Biol Chem 275: 34353-34358.
    • (2000) J Biol Chem , vol.275 , pp. 34353-34358
    • Hayashi, M.1    Yamada, H.2    Mitamura, T.3    Horii, T.4    Yamamoto, A.5
  • 32
    • 0345528107 scopus 로고    scopus 로고
    • Drug resistance-associated PfCRT mutations confer decreased Plasmodium falciparum digestive vacuolar pH
    • Bennett TN, Kosar AD, Ursos LM, Dzekunov S, Singh Sidhu AB, et al. (2004) Drug resistance-associated PfCRT mutations confer decreased Plasmodium falciparum digestive vacuolar pH. Mol Biochem Parasitol 133: 99-114.
    • (2004) Mol Biochem Parasitol , vol.133 , pp. 99-114
    • Bennett, T.N.1    Kosar, A.D.2    Ursos, L.M.3    Dzekunov, S.4    Singh Sidhu, A.B.5
  • 33
    • 33645751112 scopus 로고    scopus 로고
    • The pH of the digestive vacuole of Plasmodium falciparum is not associated with chloroquine resistance
    • Hayward R, Saliba KJ, Kirk K, (2006) The pH of the digestive vacuole of Plasmodium falciparum is not associated with chloroquine resistance. J Cell Sci 119: 1016-1025.
    • (2006) J Cell Sci , vol.119 , pp. 1016-1025
    • Hayward, R.1    Saliba, K.J.2    Kirk, K.3
  • 34
    • 33947125517 scopus 로고    scopus 로고
    • Quantitative pH measurements in Plasmodium falciparum-infected erythrocytes using pHluorin
    • Kuhn Y, Rohrbach P, Lanzer M, (2007) Quantitative pH measurements in Plasmodium falciparum-infected erythrocytes using pHluorin. Cell Microbiol 9: 1004-1013.
    • (2007) Cell Microbiol , vol.9 , pp. 1004-1013
    • Kuhn, Y.1    Rohrbach, P.2    Lanzer, M.3
  • 35
    • 84909530521 scopus 로고
    • Mononuclear phagocytes: effectors of cellular immunity and hosts for facultative intracellular pathogens
    • Boros DL, Yoshida T, editors, Amsterdam: Elsevier/North Holland
    • Silverstein SC, Michl J, Nathan CF, Horwitz MA (1980) Mononuclear phagocytes: effectors of cellular immunity and hosts for facultative intracellular pathogens. In: Boros DL, Yoshida T, editors. Basic and clinical aspects of granulomatous diseases. Amsterdam: Elsevier/North Holland. pp. 70-76.
    • (1980) Basic and clinical aspects of granulomatous diseases , pp. 70-76
    • Silverstein, S.C.1    Michl, J.2    Nathan, C.F.3    Horwitz, M.A.4
  • 36
    • 0000327692 scopus 로고    scopus 로고
    • Carbohydrate Metabolism of Asexual Stages
    • Sherman IW, editor, Washington, DC: American Society of Microbiology
    • Sherman IW (1998) Carbohydrate Metabolism of Asexual Stages. In: Sherman IW, editor. Malaria-Parasite Biology, Pathogenesis and Protection. Washington, DC: American Society of Microbiology. pp. 135-143.
    • (1998) Malaria-Parasite Biology, Pathogenesis and Protection , pp. 135-143
    • Sherman, I.W.1
  • 37
    • 0037934729 scopus 로고    scopus 로고
    • Validation of the hexose transporter of Plasmodium falciparum as a novel drug target
    • Joet T, Eckstein-Ludwig U, Morin C, Krishna S, (2003) Validation of the hexose transporter of Plasmodium falciparum as a novel drug target. Proc Natl Acad Sci USA 100: 7476-7479.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 7476-7479
    • Joet, T.1    Eckstein-Ludwig, U.2    Morin, C.3    Krishna, S.4
  • 38
    • 3142566345 scopus 로고    scopus 로고
    • Inhibition of hexose transport and abrogation of pH homeostasis in the intraerythrocytic malaria parasite by an O-3-hexose derivative
    • Saliba KJ, Krishna S, Kirk K, (2004) Inhibition of hexose transport and abrogation of pH homeostasis in the intraerythrocytic malaria parasite by an O-3-hexose derivative. FEBS Lett 570: 93-96.
    • (2004) FEBS Lett , vol.570 , pp. 93-96
    • Saliba, K.J.1    Krishna, S.2    Kirk, K.3
  • 39
    • 54249146986 scopus 로고    scopus 로고
    • Targets for hydrogen-peroxide-induced damage to suspension and biofilm cells of Streptococcus mutans
    • Baldeck JD, Marquis RE, (2008) Targets for hydrogen-peroxide-induced damage to suspension and biofilm cells of Streptococcus mutans. Can J Microbiol 54: 868-875.
    • (2008) Can J Microbiol , vol.54 , pp. 868-875
    • Baldeck, J.D.1    Marquis, R.E.2
  • 40
    • 0034321934 scopus 로고    scopus 로고
    • H2O2-induced block of glycolysis as an active ADP-ribosylation reaction protecting cells from apoptosis
    • Colussi C, Albertini MC, Coppola S, Rovidati S, Galli F, et al. (2000) H2O2-induced block of glycolysis as an active ADP-ribosylation reaction protecting cells from apoptosis. FASEB J 14: 2266-2276.
    • (2000) FASEB J , vol.14 , pp. 2266-2276
    • Colussi, C.1    Albertini, M.C.2    Coppola, S.3    Rovidati, S.4    Galli, F.5
  • 41
    • 0037394045 scopus 로고    scopus 로고
    • H2O2, but not menadione, provokes a decrease in the ATP and an increase in the inosine levels in Saccharomyces cerevisiae. An experimental and theoretical approach
    • Osorio H, Carvalho E, del Valle M, Gunther Sillero MA, Moradas-Ferreira P, et al. (2003) H2O2, but not menadione, provokes a decrease in the ATP and an increase in the inosine levels in Saccharomyces cerevisiae. An experimental and theoretical approach. Eur J Biochem 270: 1578-1589.
    • (2003) Eur J Biochem , vol.270 , pp. 1578-1589
    • Osorio, H.1    Carvalho, E.2    del Valle, M.3    Gunther Sillero, M.A.4    Moradas-Ferreira, P.5
  • 42
    • 37549072681 scopus 로고    scopus 로고
    • Dynamic rerouting of the carbohydrate flux is key to counteracting oxidative stress
    • Ralser M, Wamelink MM, Kowald A, Gerisch B, Heeren G, et al. (2007) Dynamic rerouting of the carbohydrate flux is key to counteracting oxidative stress. J Biol 6: 10.
    • (2007) J Biol , vol.6 , pp. 10
    • Ralser, M.1    Wamelink, M.M.2    Kowald, A.3    Gerisch, B.4    Heeren, G.5
  • 43
    • 0035988177 scopus 로고    scopus 로고
    • The effect of H2O2 and tertiary butyl hydroperoxide upon a murine immortal lens epithelial cell line, alphaTN4-1
    • Spector A, Ma W, Sun F, Li D, Kleiman NJ, (2002) The effect of H2O2 and tertiary butyl hydroperoxide upon a murine immortal lens epithelial cell line, alphaTN4-1. Exp Eye Res 75: 573-582.
    • (2002) Exp Eye Res , vol.75 , pp. 573-582
    • Spector, A.1    Ma, W.2    Sun, F.3    Li, D.4    Kleiman, N.J.5
  • 44
    • 0023874677 scopus 로고
    • Mechanisms of oxidant-mediated cell injury. The glycolytic and mitochondrial pathways of ADP phosphorylation are major intracellular targets inactivated by hydrogen peroxide
    • Hyslop PA, Hinshaw DB, Halsey WA Jr, Schraufstatter IU, Sauerheber RD, et al. (1988) Mechanisms of oxidant-mediated cell injury. The glycolytic and mitochondrial pathways of ADP phosphorylation are major intracellular targets inactivated by hydrogen peroxide. J Biol Chem 263: 1665-1675.
    • (1988) J Biol Chem , vol.263 , pp. 1665-1675
    • Hyslop, P.A.1    Hinshaw, D.B.2    Halsey Jr., W.A.3    Schraufstatter, I.U.4    Sauerheber, R.D.5
  • 45
    • 0028204459 scopus 로고
    • S-thiolation of human endothelial cell glyceraldehyde-3-phosphate dehydrogenase after hydrogen peroxide treatment
    • Schuppe-Koistinen I, Moldeus P, Bergman T, Cotgreave IA, (1994) S-thiolation of human endothelial cell glyceraldehyde-3-phosphate dehydrogenase after hydrogen peroxide treatment. Eur J Biochem 221: 1033-1037.
    • (1994) Eur J Biochem , vol.221 , pp. 1033-1037
    • Schuppe-Koistinen, I.1    Moldeus, P.2    Bergman, T.3    Cotgreave, I.A.4
  • 46
    • 77949357436 scopus 로고    scopus 로고
    • Life cycle studies of the hexose transporter of Plasmodium species and genetic validation of their essentiality
    • Slavic K, Straschil U, Reininger L, Doerig C, Morin C, et al. (2010) Life cycle studies of the hexose transporter of Plasmodium species and genetic validation of their essentiality. Mol Microbiol.
    • (2010) Mol Microbiol
    • Slavic, K.1    Straschil, U.2    Reininger, L.3    Doerig, C.4    Morin, C.5
  • 47
    • 1642483495 scopus 로고    scopus 로고
    • The membrane potential of the intraerythrocytic malaria parasite Plasmodium falciparum
    • Allen RJ, Kirk K, (2004) The membrane potential of the intraerythrocytic malaria parasite Plasmodium falciparum. J Biol Chem 279: 11264-11272.
    • (2004) J Biol Chem , vol.279 , pp. 11264-11272
    • Allen, R.J.1    Kirk, K.2
  • 48
    • 0034410938 scopus 로고    scopus 로고
    • Hexose transport in asexual stages of Plasmodium falciparum and kinetoplastidae
    • Krishna S, Woodrow CJ, Burchmore RJ, Saliba KJ, Kirk K, (2000) Hexose transport in asexual stages of Plasmodium falciparum and kinetoplastidae. Parasitol Today 16: 516-521.
    • (2000) Parasitol Today , vol.16 , pp. 516-521
    • Krishna, S.1    Woodrow, C.J.2    Burchmore, R.J.3    Saliba, K.J.4    Kirk, K.5
  • 49
    • 0019834321 scopus 로고
    • Properties of H+-translocating adenosine triphosphatase in vacuolar membranes of Saccharomyces cerevisiae
    • Kakinuma Y, Ohsumi Y, Anraku Y, (1981) Properties of H+-translocating adenosine triphosphatase in vacuolar membranes of Saccharomyces cerevisiae. J Biol Chem 256: 10859-10863.
    • (1981) J Biol Chem , vol.256 , pp. 10859-10863
    • Kakinuma, Y.1    Ohsumi, Y.2    Anraku, Y.3
  • 50
    • 0024342428 scopus 로고
    • Comparative studies on the electrical properties of the H+ translocating ATPase and pyrophosphatase of the vacuolar-lysosomal compartment
    • Hedrich R, Kurkdjian A, Guern J, Flugge UI, (1989) Comparative studies on the electrical properties of the H+ translocating ATPase and pyrophosphatase of the vacuolar-lysosomal compartment. EMBO J 8: 2835-2841.
    • (1989) EMBO J , vol.8 , pp. 2835-2841
    • Hedrich, R.1    Kurkdjian, A.2    Guern, J.3    Flugge, U.I.4
  • 51
    • 0023656756 scopus 로고
    • Immunoaffinity purification and characterization of vacuolar H+ATPase from bovine kidney
    • Gluck S, Caldwell J, (1987) Immunoaffinity purification and characterization of vacuolar H+ATPase from bovine kidney. J Biol Chem 262: 15780-15789.
    • (1987) J Biol Chem , vol.262 , pp. 15780-15789
    • Gluck, S.1    Caldwell, J.2
  • 52
    • 0033556401 scopus 로고    scopus 로고
    • The vacuolar H+-ATPase of clathrin-coated vesicles is reversibly inhibited by S-nitrosoglutathione
    • Forgac M, (1999) The vacuolar H+-ATPase of clathrin-coated vesicles is reversibly inhibited by S-nitrosoglutathione. J Biol Chem 274: 1301-1305.
    • (1999) J Biol Chem , vol.274 , pp. 1301-1305
    • Forgac, M.1
  • 53
    • 0031890883 scopus 로고    scopus 로고
    • Hydrogen peroxide inhibits the vacuolar H+-ATPase in brain synaptic vesicles at micromolar concentrations
    • Wang Y, Floor E, (1998) Hydrogen peroxide inhibits the vacuolar H+-ATPase in brain synaptic vesicles at micromolar concentrations. J Neurochem 70: 646-652.
    • (1998) J Neurochem , vol.70 , pp. 646-652
    • Wang, Y.1    Floor, E.2
  • 54
    • 0034782623 scopus 로고    scopus 로고
    • Reversible redox control of plant vacuolar H+-ATPase activity is related to disulfide bridge formation in subunit E as well as subunit A
    • Tavakoli N, Kluge C, Golldack D, Mimura T, Dietz KJ, (2001) Reversible redox control of plant vacuolar H+-ATPase activity is related to disulfide bridge formation in subunit E as well as subunit A. Plant J. 28: 51-59.
    • (2001) Plant J , vol.28 , pp. 51-59
    • Tavakoli, N.1    Kluge, C.2    Golldack, D.3    Mimura, T.4    Dietz, K.J.5
  • 55
    • 0028906608 scopus 로고
    • The vacuolar ATPase: sulfite stabilization and the mechanism of nitrate inactivation
    • Dschida WJ, Bowman BJ, (1995) The vacuolar ATPase: sulfite stabilization and the mechanism of nitrate inactivation. J Biol Chem 270: 1557-1563.
    • (1995) J Biol Chem , vol.270 , pp. 1557-1563
    • Dschida, W.J.1    Bowman, B.J.2
  • 56
    • 0028319319 scopus 로고
    • Inhibition of vacuolar H+-ATPase by disulfide bond formation between cysteine 254 and cysteine 532 in subunit A
    • Feng Y, Forgac M, (1994) Inhibition of vacuolar H+-ATPase by disulfide bond formation between cysteine 254 and cysteine 532 in subunit A. J Biol Chem 269: 13224-13230.
    • (1994) J Biol Chem , vol.269 , pp. 13224-13230
    • Feng, Y.1    Forgac, M.2
  • 57
    • 37849019012 scopus 로고    scopus 로고
    • Artemisinin and a series of novel endoperoxide antimalarials exert early effects on digestive vacuole morphology
    • del Pilar Crespo M, Avery TD, Hanssen E, Fox E, Robinson TV, et al. (2008) Artemisinin and a series of novel endoperoxide antimalarials exert early effects on digestive vacuole morphology. Antimicrob Agents Chemother 52: 98-109.
    • (2008) Antimicrob Agents Chemother , vol.52 , pp. 98-109
    • del Pilar Crespo, M.1    Avery, T.D.2    Hanssen, E.3    Fox, E.4    Robinson, T.V.5
  • 58
    • 77649184668 scopus 로고    scopus 로고
    • Inhibition of Plasmodium falciparum pH regulation by small molecule indole derivatives results in rapid parasite death
    • van Schalkwyk DA, Chan XW, Misiano P, Gagliardi S, Farina C, et al. (2010) Inhibition of Plasmodium falciparum pH regulation by small molecule indole derivatives results in rapid parasite death. Biochem Pharmacol 79: 1291-1299.
    • (2010) Biochem Pharmacol , vol.79 , pp. 1291-1299
    • van Schalkwyk, D.A.1    Chan, X.W.2    Misiano, P.3    Gagliardi, S.4    Farina, C.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.