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Volumn 8, Issue 1, 2009, Pages

Co-ordinated stage-dependent enhancement of Plasmodium falciparum antioxidant enzymes and heat shock protein expression in parasites growing in oxidatively stressed or G6PD-deficient red blood cells

Author keywords

[No Author keywords available]

Indexed keywords

HEAT SHOCK PROTEIN; HEAT SHOCK PROTEIN 2; HEAT SHOCK PROTEIN 3; HEAT SHOCK PROTEIN 60; HEAT SHOCK PROTEIN 70; HEAT SHOCK PROTEIN 75; HEAT SHOCK PROTEIN 90; HYDROGEN PEROXIDE; MESSENGER RNA; UNCLASSIFIED DRUG; ANTIOXIDANT; GLUCOSE 6 PHOSPHATE DEHYDROGENASE; OXIDIZING AGENT; PROTOZOAL PROTEIN;

EID: 67650723464     PISSN: None     EISSN: 14752875     Source Type: Journal    
DOI: 10.1186/1475-2875-8-113     Document Type: Article
Times cited : (47)

References (71)
  • 1
    • 0027430639 scopus 로고
    • Origin of reactive oxygen species in erythrocytes infected with Plasmodium falciparum
    • DOI 10.1016/0166-6851(93)90069-A
    • Origin of reactive oxygen species in erythrocytes infected with Plasmodium falciparum. H Atamna H Ginsburg, Mol Biochem Parasitol 1993 61 231 241 8264727 (Pubitemid 223039723)
    • (1993) Molecular and Biochemical Parasitology , vol.61 , Issue.2 , pp. 231-241
    • Atamna, H.1    Ginsburg, H.2
  • 3
    • 0037621507 scopus 로고    scopus 로고
    • Glutathione - Functions and metabolism in the malarial parasite Plasmodium falciparum
    • DOI 10.1515/BC.2003.063
    • Glutathionefunctions and metabolism in the malarial parasite Plasmodium falciparum. K Becker S Rahlfs C Nickel RH Schirmer, Biol Chem 2003 384 551 566 12751785 (Pubitemid 36609171)
    • (2003) Biological Chemistry , vol.384 , Issue.4 , pp. 551-566
    • Becker, K.1    Rahlfs, S.2    Nickel, C.3    Schirmer, R.H.4
  • 4
    • 0034161967 scopus 로고    scopus 로고
    • Plasmodium falciparum-infected red blood cells depend on a functional glutathione de novo synthesis attributable to an enhanced loss of glutathione
    • DOI 10.1042/0264-6021:3460545
    • Plasmodium falciparum-infected red blood cells depend on a functional glutathione de novo synthesis attributable to an enhanced loss of glutathione. K Lüersen RD Walter S Müller, Biochem J 2000 346 545 552 10677377 (Pubitemid 30148144)
    • (2000) Biochemical Journal , vol.346 , Issue.2 , pp. 545-552
    • Luersen, K.1    Walter, R.D.2    Muller, S.3
  • 5
    • 0037115759 scopus 로고    scopus 로고
    • Regulation of intracellular glutathione levels in erythrocytes infected with chloroquine-sensitive and chloroquine-resistant Plasmodium falciparum
    • DOI 10.1042/BJ20020962
    • Regulation of intracellular glutathione levels in erythrocytes infected with chloroquine-sensitive and chloroquine-resistant Plasmodium falciparum. S Meierjohann RD Walter S Müller, Biochem J 2002 368 761 768 12225291 (Pubitemid 36042677)
    • (2002) Biochemical Journal , vol.368 , Issue.3 , pp. 761-768
    • Meierjohann, S.1    Walter, R.D.2    Muller, S.3
  • 6
    • 0036305476 scopus 로고    scopus 로고
    • The thioredoxin system of Plasmodium falciparum and other parasites
    • DOI 10.1007/s00018-002-8484-9
    • The thioredoxin system of Plasmodium falciparum and other parasites. S Rahlfs RH Schirmer K Becker, Cell Mol Life Sci 2002 59 1024 1041 12169015 (Pubitemid 34734634)
    • (2002) Cellular and Molecular Life Sciences , vol.59 , Issue.6 , pp. 1024-1041
    • Rahlfs, S.1    Schirmer, R.H.2    Becker, K.3
  • 7
    • 4444359792 scopus 로고    scopus 로고
    • Redox and antioxidant systems of the malaria parasite Plasmodium falciparum
    • DOI 10.1111/j.1365-2958.2004.04257.x
    • Redox and antioxidant systems of the malaria parasite Plasmodium falciparum. S Müller, Mol Microbiol 2004 53 1291 1305 15387810 (Pubitemid 39209105)
    • (2004) Molecular Microbiology , vol.53 , Issue.5 , pp. 1291-1305
    • Muller, S.1
  • 8
    • 0038646796 scopus 로고    scopus 로고
    • Thiol-based redox metabolism of protozoan parasites
    • DOI 10.1016/S1471-4922(03)00141-7
    • Thiol-based redox metabolism of protozoan parasites. S Müller E Liebau RD Walter RL Krauth-Siegel, Trends Parasitol 2003 19 320 328 12855383 (Pubitemid 36829189)
    • (2003) Trends in Parasitology , vol.19 , Issue.7 , pp. 320-328
    • Muller, S.1    Liebau, E.2    Walter, R.D.3    Krauth-Siegel, R.L.4
  • 9
    • 0034844693 scopus 로고    scopus 로고
    • Glucose-6-phosphate dehydrogenase-6-phosphogluconolactonase: A novel bifunctional enzyme in malaria parasites
    • DOI 10.1046/j.1432-1327.2001.02078.x
    • Glucose-6-phosphate dehydrogenase-6-phosphogluconolactonase. A novel bifunctional enzyme in malaria parasites. JL Clarke DA Scopes O Sodeinde PJ Mason, Eur J Biochem 2001 268 2013 2019 11277923 (Pubitemid 32852942)
    • (2001) European Journal of Biochemistry , vol.268 , Issue.7 , pp. 2013-2019
    • Clarke, J.L.1    Scopes, D.A.2    Sodeinde, O.3    Mason, P.J.4
  • 12
    • 0037113995 scopus 로고    scopus 로고
    • Mitochondrial Hsp60, resistance to oxidative stress, and the labile iron pool are closely connected in Saccharomyces cerevisiae
    • DOI 10.1074/jbc.M206525200
    • Mitochondrial Hsp60, resistance to oxidative stress, and the labile iron pool are closely connected in Saccharomyces cerevisiae. E Cabiscol G Bellí J Tamarit P Echave E Herrero J Ros, J Biol Chem 2002 277 44531 44538 12200437 (Pubitemid 36157888)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.46 , pp. 44531-44538
    • Cabiscol, E.1    Belli, G.2    Tamarit, J.3    Echave, P.4    Herrero, E.5    Ros, J.6
  • 13
    • 34247513586 scopus 로고    scopus 로고
    • Chaperoning a cellular upheaval in malaria: Heat shock proteins in Plasmodium falciparum
    • DOI 10.1016/j.molbiopara.2007.01.009, PII S0166685107000369
    • Chaperoning a cellular upheaval in malaria: heat shock proteins in Plasmodium falciparum. P Acharya R Kumar U Tatu, Mol Biochem Parasitol 2007 153 85 94 17307260 (Pubitemid 46654240)
    • (2007) Molecular and Biochemical Parasitology , vol.153 , Issue.2 , pp. 85-94
    • Acharya, P.1    Kumar, R.2    Tatu, U.3
  • 14
    • 34848844683 scopus 로고    scopus 로고
    • Systems analysis of chaperone networks in the malarial parasite Plasmodium falciparum
    • DOI 10.1371/journal.pcbi.0030168
    • Systems analysis of chaperone networks in the malarial parasite Plasmodium falciparum. SR Pavithra R Kumar U Tatu, PLoS Comput Biol 2007 3 1701 1715 17941702 (Pubitemid 47502975)
    • (2007) PLoS Computational Biology , vol.3 , Issue.9 , pp. 1701-1715
    • Pavithra, S.R.1    Kumar, R.2    Tatu, U.3
  • 15
    • 57649177187 scopus 로고    scopus 로고
    • Heat-shock proteins (Review)
    • Appendix 1-Appendix 1T 18432918
    • Heat-shock proteins (Review). Z Li P Srivastava, Curr Protoc Immunol 2004 Appendix 1-Appendix 1T 18432918
    • (2004) Curr Protoc Immunol
    • Li, Z.1    Srivastava, P.2
  • 16
    • 33646010643 scopus 로고    scopus 로고
    • Chaperones in preventing protein denaturation in living cells and protecting against cellular stress
    • 16610353
    • Chaperones in preventing protein denaturation in living cells and protecting against cellular stress. HH Kampinga, Handb Exp Pharmacol 2006 172 1 42 16610353
    • (2006) Handb Exp Pharmacol , vol.172 , pp. 1-42
    • Kampinga, H.H.1
  • 17
    • 0037009130 scopus 로고    scopus 로고
    • Molecular chaperones as essential mediators of mitochondrial biogenesis (Review)
    • 12191768
    • Molecular chaperones as essential mediators of mitochondrial biogenesis (Review). W Voss K Rttgers, Biochim Biophys Acta 2002 1592 51 62 12191768
    • (2002) Biochim Biophys Acta , vol.1592 , pp. 51-62
    • Voss, W.1    Rttgers, K.2
  • 18
    • 37849022851 scopus 로고    scopus 로고
    • Mitochondrial stress signaling: A pathway unfolds
    • 18068368
    • Mitochondrial stress signaling: a pathway unfolds. SA Broadley FU Hartl, Trends Cell Biol 2007 18 1 4 18068368
    • (2007) Trends Cell Biol , vol.18 , pp. 1-4
    • Broadley, S.A.1    Hartl, F.U.2
  • 19
    • 0033519627 scopus 로고    scopus 로고
    • Oxidative stress: Protein folding with a novel redox switch
    • 10359689
    • Oxidative stress: Protein folding with a novel redox switch. LW Ruddock P Klappa, Curr Biol 1999 9 R400 402 10359689
    • (1999) Curr Biol , vol.9 , pp. 400-402
    • Ruddock, L.W.1    Klappa, P.2
  • 20
    • 0142075876 scopus 로고    scopus 로고
    • Molecular chaperones, stress proteins and redox homeostasis
    • Molecular chaperones, stress proteins and redox homeostasis. E Papp G Nardai C Soti P Csermely, Biofactors 2003 17 249 257 12897446 (Pubitemid 37267159)
    • (2003) BioFactors , vol.17 , Issue.1-4 , pp. 249-257
    • Papp, E.1    Nardai, G.2    Soti, C.3    Csermely, P.4
  • 21
    • 0036865082 scopus 로고    scopus 로고
    • Hsp70, an immunological actor playing with the intracellular self under oxidative stress
    • DOI 10.1080/02656730210146926
    • Hsp70, an immunological actor playing with the intracellular self under oxidative stress. A Menoret D Chaillot M Callahan C Jacquin, Int J Hyperthermia 2002 18 490 505 12537750 (Pubitemid 35469183)
    • (2002) International Journal of Hyperthermia , vol.18 , Issue.6 , pp. 490-505
    • Menoret, A.1    Chaillot, D.2    Callahan, M.3    Jacquin, C.4
  • 22
    • 0032527963 scopus 로고    scopus 로고
    • Protection from oxidative inactivation of the 20 S proteasome by heat-shock protein 90
    • Protection from oxidative inactivation of the 20S proteasome by heat-shock protein 90. M Conconi I Petropoulos I Emod E Turlin F Biville B Friguet, Biochem J 1998 333 407 415 9657982 (Pubitemid 28379544)
    • (1998) Biochemical Journal , vol.333 , Issue.2 , pp. 407-415
    • Conconi, M.1    Petropoulos, I.2    Emod, I.3    Turlin, E.4    Biville, F.5    Friguet, B.6
  • 23
    • 0027311128 scopus 로고
    • Oxygen free radicals as inducers of heat shock protein synthesis in cultured human neuroblastoma cells: Relevance to neurodegenerative disease
    • Oxygen free radicals as inducers of heat shock protein synthesis in cultured human neuroblastoma cells: relevance to neurodegenerative disease. R Omar M Pappolla, Eur Arch Psychiatry Clin Neurosci 1993 242 262 267 8499494 (Pubitemid 23191737)
    • (1993) European Archives of Psychiatry and Clinical Neuroscience , vol.242 , Issue.5 , pp. 262-267
    • Omar, R.1    Pappolla, M.2
  • 24
    • 35348905486 scopus 로고    scopus 로고
    • Heat shock protein 70 regulates cellular redox status by modulating glutathione-related enzyme activities
    • DOI 10.1379/CSC-265.1
    • Heat shock protein 70 regulates cellular redox status by modulating glutathione-related enzyme activities. S Guo W Wharton P Moseley H Shi, Cell Stress Chaperones 2007 12 245 254 17915557 (Pubitemid 351199387)
    • (2007) Cell Stress and Chaperones , vol.12 , Issue.3 , pp. 245-254
    • Guo, S.1    Wharton, W.2    Moseley, P.3    Shi, H.4
  • 25
  • 26
    • 0037021405 scopus 로고    scopus 로고
    • Artemisinin: Mechanisms of action, resistance and toxicity
    • DOI 10.1016/S0020-7519(02)00194-7, PII S0020751902001947
    • Artemisinin: mechanisms of action, resistance and toxicity. SR Meshnick, Int J Parasitol 2002 32 1655 1660 12435450 (Pubitemid 35339455)
    • (2002) International Journal for Parasitology , vol.32 , Issue.13 , pp. 1655-1660
    • Meshnick, S.R.1
  • 27
    • 1142297431 scopus 로고    scopus 로고
    • Ferriprotoporphyrin IX, phospholipids, and the antimalarial actions of quinoline drugs
    • DOI 10.1016/j.lfs.2003.10.003
    • Ferriprotoporphyrin IX, phospholipids, and the antimalarial actions of quinoline drugs. CD Fitch, Life Sci 2004 74 1957 1972 14967191 (Pubitemid 38210349)
    • (2004) Life Sciences , vol.74 , Issue.16 , pp. 1957-1972
    • Fitch, C.D.1
  • 30
    • 0032189018 scopus 로고    scopus 로고
    • Early phagocytosis of glucose-6-phosphate dehydrogenase (G6PD)-deficient erythrocytes parasitized by Plasmodium falciparum may explain malaria protection in G6PD deficiency
    • Early phagocytosis of glucose-6-phosphate dehydrogenase (G6PD)-deficient erythrocytes parasitized by Plasmodium falciparum may explain malaria protection in G6PD deficiency. M Cappadoro G Giribaldi E O'Brien F Turrini F Mannu D Ulliers G Simula L Luzzatto P Arese, Blood 1998 92 2527 2534 9746794 (Pubitemid 28452997)
    • (1998) Blood , vol.92 , Issue.7 , pp. 2527-2534
    • Cappadoro, M.1    Giribaldi, G.2    O'Brien, E.3    Turrini, F.4    Mannu, F.5    Ulliers, D.6    Simula, G.7    Luzzatto, L.8    Arese, P.9
  • 31
    • 8644226200 scopus 로고    scopus 로고
    • Enhanced phagocytosis of ring-parasitized mutant erythrocytes: A common mechanism that may explain protection against falciparum malaria in sickle trait and beta-thalassemia trait
    • DOI 10.1182/blood-2003-11-3820
    • Enhanced phagocytosis of ring-parasitized mutant erythrocytes: a common mechanism that may explain protection against falciparum malaria in sickle trait and beta-thalassemia trait. K Ayi F Turrini A Piga P Arese, Blood 2004 104 3364 3371 15280204 (Pubitemid 39507160)
    • (2004) Blood , vol.104 , Issue.10 , pp. 3364-3371
    • Ayi, K.1    Turrini, F.2    Piga, A.3    Arese, P.4
  • 32
    • 0024584529 scopus 로고
    • Metabolic interconnection between the human malarial parasite Plasmodium falciparum and its host erythrocyte. Regulation of ATP levels by means of an adenylate translocator and adenylate kinase
    • Metabolic interconnection between the human malarial parasite Plasmodium falciparum and its host erythrocyte. Regulation of ATP levels by means of an adenylate translocator and adenylate kinase. J Kanaani H Ginsburg, J Biol Chem 1989 264 3194 3199 2536737 (Pubitemid 19063376)
    • (1989) Journal of Biological Chemistry , vol.264 , Issue.6 , pp. 3194-3199
    • Kanaani, J.1    Ginsburg, H.2
  • 33
    • 0016196643 scopus 로고
    • The mechanism of action of xanthine oxidase
    • 4367215
    • The mechanism of action of xanthine oxidase. JS Olson DP Ballou G Palmer V Massey, J Biol Chem 1974 249 4363 4382 4367215
    • (1974) J Biol Chem , vol.249 , pp. 4363-4382
    • Olson, J.S.1    Ballou, D.P.2    Palmer, G.3    Massey, V.4
  • 34
    • 0032861181 scopus 로고    scopus 로고
    • Application and modulation of a permanent hydrogen peroxide-induced oxidative stress to cultured astroglial cells
    • DOI 10.1016/S1385-299X(99)00023-9, PII S1385299X99000239
    • Application and modulation of a permanent hydrogen peroxide-induced oxidative stress to cultured astroglial cells. J Hirrlinger B Hamprecht R Dringen, Brain Res Brain Res Protoc 1999 4 223 229 10446418 (Pubitemid 29396423)
    • (1999) Brain Research Protocols , vol.4 , Issue.2 , pp. 223-229
    • Hirrlinger, J.1    Hamprecht, B.2    Dringen, R.3
  • 35
    • 0014939684 scopus 로고
    • On the mechanism of inactivation of xanthine oxidase by allopurinol and other pyrazolo[3,4-d]pyrimidines
    • 5467924
    • On the mechanism of inactivation of xanthine oxidase by allopurinol and other pyrazolo[3,4-d]pyrimidines. V Massey H Komai G Palmer GB Elion, J Biol Chem 1970 245 2837 2844 5467924
    • (1970) J Biol Chem , vol.245 , pp. 2837-2844
    • Massey, V.1    Komai, H.2    Palmer, G.3    Elion, G.B.4
  • 36
    • 0035710746 scopus 로고    scopus 로고
    • -ΔΔCT method
    • DOI 10.1006/meth.2001.1262
    • Analysis of relative gene expression data using real-time quantitative PCR and the 2(-Delta Delta C(T)) method. KJ Livak TD Schmittgen, Methods 2001 25 402 408 11846609 (Pubitemid 34164012)
    • (2001) Methods , vol.25 , Issue.4 , pp. 402-408
    • Livak, K.J.1    Schmittgen, T.D.2
  • 39
    • 34548232285 scopus 로고    scopus 로고
    • The Hsp40 proteins of Plasmodium falciparum and other apicomplexa: Regulating chaperone power in the parasite and the host
    • DOI 10.1016/j.biocel.2007.02.011, PII S1357272507000581
    • The Hsp40 proteins of Plasmodium falciparum and other apicomplexa: regulating chaperone power in the parasite and the host. M Botha ER Pesce GL Blatch, Int J Biochem Cell Biol 2007 39 1781 1803 17428722 (Pubitemid 47321340)
    • (2007) International Journal of Biochemistry and Cell Biology , vol.39 , Issue.10 , pp. 1781-1803
    • Botha, M.1    Pesce, E.-R.2    Blatch, G.L.3
  • 40
    • 0030200510 scopus 로고    scopus 로고
    • Cloning of a Plasmodium falciparum gene related to the human 60-kDa heat shock protein
    • DOI 10.1016/0166-6851(96)02633-3
    • Cloning of a Plasmodium falciparum gene related to the human 60-kDa heat shock protein. C Syin ND Goldman, Mol Biochem Parasitol 1996 79 13 19 8844668 (Pubitemid 26241901)
    • (1996) Molecular and Biochemical Parasitology , vol.79 , Issue.1 , pp. 13-19
    • Syin, C.1    Goldman, N.D.2
  • 41
    • 0842267072 scopus 로고    scopus 로고
    • Overproduction, purification, and characterization of the Plasmodium falciparum heat shock protein 70
    • DOI 10.1016/j.pep.2003.09.010
    • Overproduction, purification, and characterization of the Plasmodium falciparum heat shock protein 70. TS Matambo OO Odunuga A Boshoff GL Blatch, Protein Expr Purif 2004 33 214 222 14711509 (Pubitemid 38161987)
    • (2004) Protein Expression and Purification , vol.33 , Issue.2 , pp. 214-222
    • Matambo, T.S.1    Odunuga, O.O.2    Boshoff, A.3    Blatch, G.L.4
  • 42
    • 34248216407 scopus 로고    scopus 로고
    • Three-dimensional structure of heat shock protein 90 from Plasmodium falciparum: Molecular modelling approach to rational drug design against malaria
    • DOI 10.1007/s12038-007-0052-x
    • Three-dimensional structure of heat shock protein 90 from Plasmodium falciparum: molecular modelling approach to rational drug design against malaria. R Kumar SR Pavithra U Tatu, J Biosci 2007 32 531 536 17536172 (Pubitemid 46708703)
    • (2007) Journal of Biosciences , vol.32 , Issue.3 , pp. 531-536
    • Kumar, R.1    Pavithra, S.R.2    Tatu, U.3
  • 43
    • 0038381514 scopus 로고    scopus 로고
    • Heat shock protein 90 function is essential for Plasmodium falciparum growth in human erythrocytes
    • DOI 10.1074/jbc.M211309200
    • Heat shock protein 90 function is essential for Plasmodium falciparum growth in human erythrocytes. G Banumathy V Singh SR Pavithra U Tatu, J Biol Chem 2003 278 18336 18345 12584193 (Pubitemid 36799454)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.20 , pp. 18336-18345
    • Banumathy, G.1    Singh, V.2    Pavithra, S.R.3    Tatu, U.4
  • 44
    • 3042541530 scopus 로고    scopus 로고
    • The heat shock protein 90 of Plasmodium falciparum and antimalarial activity of its inhibitor, geldanamycin
    • 14514358
    • The heat shock protein 90 of Plasmodium falciparum and antimalarial activity of its inhibitor, geldanamycin. R Kumar A Musiyenko S Barik, Malar J 2003 2 30 14514358
    • (2003) Malar J , vol.2 , pp. 30
    • Kumar, R.1    Musiyenko, A.2    Barik, S.3
  • 46
    • 4243071596 scopus 로고    scopus 로고
    • The transcriptome of the intraerythrocytic developmental cycle of Plasmodium falciparum
    • 12929205
    • The transcriptome of the intraerythrocytic developmental cycle of Plasmodium falciparum. Z Bozdech M Llinas BL Pulliam ED Wong J Zhu JL DeRisi, PLoS Biol 2003 1 E5 12929205
    • (2003) PLoS Biol , vol.1 , pp. 5
    • Bozdech, Z.1    Llinas, M.2    Pulliam, B.L.3    Wong, E.D.4    Zhu, J.5    Derisi, J.L.6
  • 47
    • 4844223479 scopus 로고    scopus 로고
    • Antioxidant defense in Plasmodium falciparumdata mining of the transcriptome
    • 15245577
    • Antioxidant defense in Plasmodium falciparumdata mining of the transcriptome. Z Bozdech H Ginsburg, Malar J 2004 3 23 15245577
    • (2004) Malar J , vol.3 , pp. 23
    • Bozdech, Z.1    Ginsburg, H.2
  • 48
    • 19344365153 scopus 로고    scopus 로고
    • Data mining of the transcriptome of Plasmodium falciparum: The pentose phosphate pathway and ancillary processes
    • 15774020
    • Data mining of the transcriptome of Plasmodium falciparum: the pentose phosphate pathway and ancillary processes. Z Bozdech H Ginsburg, Malar J 2005 4 17 15774020
    • (2005) Malar J , vol.4 , pp. 17
    • Bozdech, Z.1    Ginsburg, H.2
  • 51
    • 17144439425 scopus 로고    scopus 로고
    • 2-Cys peroxiredoxin PfTrx-Px1 is involved in the antioxidant defence of Plasmodium falciparum
    • DOI 10.1016/S0166-6851(03)00161-0
    • 2-Cys peroxiredoxin Pf Trx-Px1 is involved in the antioxidant defence of Plasmodium falciparum. SE Akerman S Müller, Mol Biochem Parasitol 2003 130 75 81 12946843 (Pubitemid 37289125)
    • (2003) Molecular and Biochemical Parasitology , vol.130 , Issue.2 , pp. 75-81
    • Akerman, S.E.1    Muller, S.2
  • 52
    • 58549094894 scopus 로고    scopus 로고
    • Control of gene expression in Plasmodium falciparum Ten years on
    • 19110008
    • Control of gene expression in Plasmodium falciparum Ten years on. P Horrocks E Wong K Russell RD Emes, Mol Biochem Parasitol 2009 164 9 25 19110008
    • (2009) Mol Biochem Parasitol , vol.164 , pp. 9-25
    • Horrocks, P.1    Wong, E.2    Russell, K.3    Emes, R.D.4
  • 54
    • 0022976939 scopus 로고
    • Regulation of glucose-6-phosphate dehydrogenase in human erythrocytes
    • Regulation of glucose-6-phosphate dehydrogenase in human erythrocytes. HN Kirkman GF Gaetani, J Biol Chem 1986 261 4033 4038 3081513 (Pubitemid 17198830)
    • (1986) Journal of Biological Chemistry , vol.261 , Issue.9 , pp. 4033-4038
    • Kirkman, H.N.1    Gaetani, G.F.2
  • 55
    • 0015918157 scopus 로고
    • Hemolytic anemia and G6PD deficiency
    • 4405605
    • Hemolytic anemia and G6PD deficiency. A Yoshida, Science 1973 179 532 537 4405605
    • (1973) Science , vol.179 , pp. 532-537
    • Yoshida, A.1
  • 56
    • 0025166591 scopus 로고
    • Pathophysiology of hemolysis in glucose-6-phosphate dehydrogenase deficiency
    • Pathophysiology of hemolysis in glucose-6-phosphate dehydrogenase deficiency. P Arese A De Flora, Semin Hematol 1990 27 1 40 2405494 (Pubitemid 20033161)
    • (1990) Seminars in Hematology , vol.27 , Issue.1 , pp. 1-40
    • Arese, P.1    De Flora, A.2
  • 57
    • 0032513245 scopus 로고    scopus 로고
    • Plasmodium falciparum glutathione metabolism and growth are independent of glutathione system of host erythrocyte
    • DOI 10.1016/S0014-5793(98)00185-9, PII S0014579398001859
    • Plasmodium falciparum glutathione metabolism and growth are independent of glutathione system of host erythrocyte. K Ayi M Cappadoro M Branca F Turrini P Arese, FEBS Lett 1998 424 257 261 9539162 (Pubitemid 28135325)
    • (1998) FEBS Letters , vol.424 , Issue.3 , pp. 257-261
    • Ayi, K.1    Cappadoro, M.2    Branca, M.3    Turrini, F.4    Arese, P.5
  • 58
    • 0037438687 scopus 로고    scopus 로고
    • Malaria-parasitized erythrocytes and hemozoin nonenzymatically generate large amounts of hydroxy fatty acids that inhibit monocyte functions
    • DOI 10.1182/blood-2002-03-0979
    • Malaria-parasitized erythrocytes and hemozoin nonenzymatically generate large amounts of hydroxy fatty acids that inhibit monocyte functions. E Schwarzer H Kuhn E Valente P Arese, Blood 2003 101 722 728 12393662 (Pubitemid 36077599)
    • (2003) Blood , vol.101 , Issue.2 , pp. 722-728
    • Schwarzer, E.1    Kuhn, H.2    Valente, E.3    Arese, P.4
  • 59
    • 0027258292 scopus 로고
    • Oxidative stress and Trichomonas vaginalis: The effect of hydrogen peroxide in vitro
    • Oxidative stress and Trichomonas vaginalis: the effect of hydrogen peroxide in vitro. SR Davis WB Lushbaugh, Am J Trop Med Hyg 1993 48 480 487 8480855 (Pubitemid 23141282)
    • (1993) American Journal of Tropical Medicine and Hygiene , vol.48 , Issue.4 , pp. 480-487
    • Davis, S.R.1    Lushbaugh, W.B.2
  • 60
    • 0028114539 scopus 로고
    • Response of Leishmania chagasi promastigotes to oxidant stress
    • Response of Leishmania chagasi promastigotes to oxidant stress. ME Wilson KA Andersen BE Britigan, Infect Immun 1994 62 5133 5141 7927797 (Pubitemid 24332824)
    • (1994) Infection and Immunity , vol.62 , Issue.11 , pp. 5133-5141
    • Wilson, M.E.1    Andersen, K.A.2    Britigan, B.E.3
  • 62
    • 58149339918 scopus 로고    scopus 로고
    • Large-scale differential proteome analysis in Plasmodium falciparum under drug treatment
    • 19116658
    • Large-scale differential proteome analysis in Plasmodium falciparum under drug treatment. JH Prieto S Koncarevic SK Park J Yates 3rd K Becker, PLoS ONE. 2008 3 12 e4098 19116658
    • (2008) PLoS ONE. , vol.3 , Issue.12 , pp. 4098
    • Prieto, J.H.1    Koncarevic, S.2    Park, S.K.3    Yates III, J.4    Becker, K.5
  • 63
    • 43849112193 scopus 로고    scopus 로고
    • Chloroquine mediates specific proteome oxidative damage across the erythrocytic cycle of resistant Plasmodium falciparum
    • 18397762
    • Chloroquine mediates specific proteome oxidative damage across the erythrocytic cycle of resistant Plasmodium falciparum. A Radfar A Diez JM Bautista, Free Radic Biol Med 2008 44 2034 2042 18397762
    • (2008) Free Radic Biol Med , vol.44 , pp. 2034-2042
    • Radfar, A.1    Diez, A.2    Bautista, J.M.3
  • 65
    • 1642554364 scopus 로고    scopus 로고
    • Identification of regulatory elements in the Plasmodium falciparum genome
    • DOI 10.1016/j.molbiopara.2003.11.004
    • Identification of regulatory elements in the Plasmodium falciparum genome. KT Militello M Dodge L Bethke DF Wirth, Mol Biochem Parasitol 2004 134 75 88 14747145 (Pubitemid 38121520)
    • (2004) Molecular and Biochemical Parasitology , vol.134 , Issue.1 , pp. 75-88
    • Militello, K.T.1    Dodge, M.2    Bethke, L.3    Wirth, D.F.4
  • 67
    • 33846811737 scopus 로고    scopus 로고
    • HNE produced by the malaria parasite Plasmodium falciparum generates HNE-protein adducts and decreases erythrocyte deformability
    • DOI 10.1179/135100007X162284
    • HNE produced by the malaria parasite Plasmodium falciparum generates HNE-protein adducts and decreases erythrocyte deformability. A Skorokhod E Schwarzer G Gremo P Arese, Redox Rep 2007 12 73 75 17263914 (Pubitemid 46210360)
    • (2007) Redox Report , vol.12 , Issue.1-2 , pp. 73-75
    • Skorokhod, A.1    Schwarzer, E.2    Gremo, G.3    Arese, P.4
  • 68
    • 36348938843 scopus 로고    scopus 로고
    • L
    • DOI 10.1074/jbc.M706799200
    • Heat shock factor 1 attenuates 4-hydroxynonenal-mediated apoptosis: critical role for heat shock protein 70 induction and stabilization of Bcl-XL. AT Jacobs LJ Marnett, J Biol Chem 2007 282 33412 33420 17873279 (Pubitemid 350159530)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.46 , pp. 33412-33420
    • Jacobs, A.T.1    Marnett, L.J.2
  • 69
    • 34447507818 scopus 로고    scopus 로고
    • Inhibitors of the heat shock response: Biology and pharmacology
    • DOI 10.1016/j.febslet.2007.05.040, PII S0014579307005686, Cellular Stress
    • Inhibitors of the heat shock response: biology and pharmacology. MV Powers P Workman, FEBS Lett 2007 581 3758 3769 17559840 (Pubitemid 47081010)
    • (2007) FEBS Letters , vol.581 , Issue.19 , pp. 3758-3769
    • Powers, M.V.1    Workman, P.2
  • 70
    • 34247490699 scopus 로고    scopus 로고
    • Relative and absolute configuration of versipelostatin, a down-regulator of molecular chaperone GRP78 expression
    • 17352484
    • Relative and absolute configuration of versipelostatin, a down-regulator of molecular chaperone GRP78 expression. HR Park S Chijiwa K Furihata Y Hayakawa K Shin-Ya, Org Lett 2007 9 1457 1460 17352484
    • (2007) Org Lett , vol.9 , pp. 1457-1460
    • Park, H.R.1    Chijiwa, S.2    Furihata, K.3    Hayakawa, Y.4    Shin-Ya, K.5
  • 71


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