메뉴 건너뛰기




Volumn 59, Issue 2, 2010, Pages 298-302

Target proteins of the cytosolic thioredoxin in Plasmodium falciparum

Author keywords

Plasmodium falciparum; Redox regulation; Thioredoxin

Indexed keywords

ACTIN; CYSTEINE; DEAD BOX PROTEIN; DISULFIDE; ELONGATION FACTOR 1ALPHA; ELONGATION FACTOR 2; GENE PRODUCT; GLYCERALDEHYDE 3 PHOSPHATE DEHYDROGENASE; HEXOKINASE; INOSINATE DEHYDROGENASE; LACTATE DEHYDROGENASE; METHIONINE ADENOSYLTRANSFERASE; MITOCHONDRIAL RNA; MUTANT PROTEIN; PEROXIREDOXIN 1; PHOSPHATIDYLINOSITOL GLYCAN BIOSYNTHESIS CLASS O PROTEIN; PHOSPHOGLYCERATE MUTASE; PROTEIN CG4; PROTEIN SERINE THREONINE KINASE; RIBONUCLEOTIDE DIPHOSPHATE REDUCTASE SUBUNIT; RIBONUCLEOTIDE REDUCTASE; RIBOSOME RNA; RNA HELICASE; THIOREDOXIN; TRYPSIN; UNCLASSIFIED DRUG;

EID: 77951620240     PISSN: 13835769     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.parint.2010.03.005     Document Type: Article
Times cited : (15)

References (38)
  • 2
    • 4444359792 scopus 로고    scopus 로고
    • Redox and antioxidant systems of the malaria parasite Plasmodium falciparum
    • Müller S. Redox and antioxidant systems of the malaria parasite Plasmodium falciparum. Mol Microbiol 53 (2004) 1291-1305
    • (2004) Mol Microbiol , vol.53 , pp. 1291-1305
    • Müller, S.1
  • 3
    • 0346398321 scopus 로고    scopus 로고
    • Thiol-dependent peroxidases care little about homology-based assignments of function
    • Flohé L., Jaeger T., Pilawa S., and Sztajer H. Thiol-dependent peroxidases care little about homology-based assignments of function. Redox Rep 8 (2003) 256-264
    • (2003) Redox Rep , vol.8 , pp. 256-264
    • Flohé, L.1    Jaeger, T.2    Pilawa, S.3    Sztajer, H.4
  • 4
    • 13444280474 scopus 로고    scopus 로고
    • Dithiol proteins as guardians of the intracellular redox milieu in parasites: old and new drug targets in trypanosomes and malaria-causing plasmodia
    • Krauth-Siegel R.L., Bauer H., and Schirmer R.H. Dithiol proteins as guardians of the intracellular redox milieu in parasites: old and new drug targets in trypanosomes and malaria-causing plasmodia. Angew Chem Int Ed Engl 44 (2005) 690-715
    • (2005) Angew Chem Int Ed Engl , vol.44 , pp. 690-715
    • Krauth-Siegel, R.L.1    Bauer, H.2    Schirmer, R.H.3
  • 5
  • 6
    • 0024393963 scopus 로고
    • Thioredoxin and glutaredoxin systems
    • Holmgren A. Thioredoxin and glutaredoxin systems. J Biol Chem 246 (1989) 13963-13966
    • (1989) J Biol Chem , vol.246 , pp. 13963-13966
    • Holmgren, A.1
  • 7
    • 0000385805 scopus 로고    scopus 로고
    • Isoforms of mammalian peroxiredoxin that reduce peroxides in presence of thioredoxin
    • Chae H.Z., Kang S.W., and Rhee S.G. Isoforms of mammalian peroxiredoxin that reduce peroxides in presence of thioredoxin. Methods Enzymol 300 (1999) 219-226
    • (1999) Methods Enzymol , vol.300 , pp. 219-226
    • Chae, H.Z.1    Kang, S.W.2    Rhee, S.G.3
  • 8
    • 0035949574 scopus 로고    scopus 로고
    • Comprehensive survey of proteins targeted by chloroplast thioredoxin
    • Motohashi K., Kondoh A., Stumpp M.T., and Hisabori T. Comprehensive survey of proteins targeted by chloroplast thioredoxin. Proc Natl Acad Sci U S A 98 (2001) 11224-11229
    • (2001) Proc Natl Acad Sci U S A , vol.98 , pp. 11224-11229
    • Motohashi, K.1    Kondoh, A.2    Stumpp, M.T.3    Hisabori, T.4
  • 10
    • 0034704081 scopus 로고    scopus 로고
    • The thioredoxin system of the malaria parasite Plasmodium falciparum. Glutathione reduction revisited
    • Kanzok S.M., Schirmer R.H., Türbachova I., Iozef R., and Becker K. The thioredoxin system of the malaria parasite Plasmodium falciparum. Glutathione reduction revisited. J Biol Chem 275 (2000) 40180-40186
    • (2000) J Biol Chem , vol.275 , pp. 40180-40186
    • Kanzok, S.M.1    Schirmer, R.H.2    Türbachova, I.3    Iozef, R.4    Becker, K.5
  • 11
    • 13844267219 scopus 로고    scopus 로고
    • Expression of mRNAs and proteins for peroxiredoxins in Plasmodium falciparum erythrocytic stage
    • Yano K., Komaki-Yasuda K., Kobayashi T., Takemae H., Kita K., Kano S., et al. Expression of mRNAs and proteins for peroxiredoxins in Plasmodium falciparum erythrocytic stage. Parasitol Int 54 (2005) 35-41
    • (2005) Parasitol Int , vol.54 , pp. 35-41
    • Yano, K.1    Komaki-Yasuda, K.2    Kobayashi, T.3    Takemae, H.4    Kita, K.5    Kano, S.6
  • 12
    • 33746505480 scopus 로고    scopus 로고
    • Structural and biochemical characterization of a mitochondrial peroxiredoxin from Plasmodium falciparum
    • Boucher I.W., McMillan P.J., Gabrielsen M., Akerman S.E., Brannigan J.A., Schnick C., et al. Structural and biochemical characterization of a mitochondrial peroxiredoxin from Plasmodium falciparum. Mol Microbiol 61 (2006) 948-959
    • (2006) Mol Microbiol , vol.61 , pp. 948-959
    • Boucher, I.W.1    McMillan, P.J.2    Gabrielsen, M.3    Akerman, S.E.4    Brannigan, J.A.5    Schnick, C.6
  • 15
    • 66349103376 scopus 로고    scopus 로고
    • Identification of proteins targeted by the thioredoxin superfamily in Plasmodium falciparum
    • Sturm N., Jortzik E., Mailu B.M., Koncarevic S., Deponte M., Forchhammer K., et al. Identification of proteins targeted by the thioredoxin superfamily in Plasmodium falciparum. PLos Pathog 5 (2009) e1000383
    • (2009) PLos Pathog , vol.5
    • Sturm, N.1    Jortzik, E.2    Mailu, B.M.3    Koncarevic, S.4    Deponte, M.5    Forchhammer, K.6
  • 16
    • 36149001369 scopus 로고    scopus 로고
    • Peroxiredoxins in malaria parasites: parasitologic aspects
    • Kawazu S., Komaki-Yasuda K., Oku H., and Kano S. Peroxiredoxins in malaria parasites: parasitologic aspects. Parasitol Int 57 (2008) 1-7
    • (2008) Parasitol Int , vol.57 , pp. 1-7
    • Kawazu, S.1    Komaki-Yasuda, K.2    Oku, H.3    Kano, S.4
  • 17
    • 12844253100 scopus 로고    scopus 로고
    • Anti-oxidative stress system in cyanobacteria. Significance of type II peroxiredoxin and the role of 1-Cys peroxiredoxin in Synechocystis sp. strain PCC 6803
    • Hosoya-Matsuda N., Motohashi K., Yoshimura H., Nozaki A., Inoue K., Ohmori M., et al. Anti-oxidative stress system in cyanobacteria. Significance of type II peroxiredoxin and the role of 1-Cys peroxiredoxin in Synechocystis sp. strain PCC 6803. J Biol Chem 280 (2005) 840-846
    • (2005) J Biol Chem , vol.280 , pp. 840-846
    • Hosoya-Matsuda, N.1    Motohashi, K.2    Yoshimura, H.3    Nozaki, A.4    Inoue, K.5    Ohmori, M.6
  • 18
    • 69449106780 scopus 로고    scopus 로고
    • The malaria parasite Plasmodium falciparum imports the human protein peroxiredoxin 2 for peroxide detoxification
    • Koncarevic C., Rohrbach P., Deponte M., Krohne G., Prieto J.H., Yates III J., et al. The malaria parasite Plasmodium falciparum imports the human protein peroxiredoxin 2 for peroxide detoxification. Proc Natl Acad Sci U S A 106 (2009) 13323-13328
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 13323-13328
    • Koncarevic, C.1    Rohrbach, P.2    Deponte, M.3    Krohne, G.4    Prieto, J.H.5    Yates III, J.6
  • 19
    • 0029841946 scopus 로고    scopus 로고
    • Effect of oxidative stress, produced by cumene hydroperoxide, on the various steps of protein synthesis. Modifications of elongation factor-2
    • Ayala A., Parrado J., Bougria M., and Machado A. Effect of oxidative stress, produced by cumene hydroperoxide, on the various steps of protein synthesis. Modifications of elongation factor-2. J Biol Chem 271 (1996) 23105-23110
    • (1996) J Biol Chem , vol.271 , pp. 23105-23110
    • Ayala, A.1    Parrado, J.2    Bougria, M.3    Machado, A.4
  • 20
    • 0033787256 scopus 로고    scopus 로고
    • Redox-regulated RNA helicase expression
    • Kujat S.L., and Owttrim G.W. Redox-regulated RNA helicase expression. Plant Physiol 124 (2000) 703-713
    • (2000) Plant Physiol , vol.124 , pp. 703-713
    • Kujat, S.L.1    Owttrim, G.W.2
  • 21
    • 0031589733 scopus 로고    scopus 로고
    • Complex polymorphisms in an 330 kDa protein are linked to chloroquine-resistant P. falciparum in Southeast Asia and Africa
    • Su X., Kirkman L.A., Fujioka H., and Wellems T.E. Complex polymorphisms in an 330 kDa protein are linked to chloroquine-resistant P. falciparum in Southeast Asia and Africa. Cell 91 (1997) 593-603
    • (1997) Cell , vol.91 , pp. 593-603
    • Su, X.1    Kirkman, L.A.2    Fujioka, H.3    Wellems, T.E.4
  • 22
    • 0028292059 scopus 로고
    • Mechanism of light modulation: identification of potential redox-sensitive cysteines distal to catalytic site in light-activated chloroplast enzymes
    • Li D., Stevens F.J., Schiffer M., and Anderson L.E. Mechanism of light modulation: identification of potential redox-sensitive cysteines distal to catalytic site in light-activated chloroplast enzymes. Biophys J 67 (1994) 29-35
    • (1994) Biophys J , vol.67 , pp. 29-35
    • Li, D.1    Stevens, F.J.2    Schiffer, M.3    Anderson, L.E.4
  • 23
    • 0021891877 scopus 로고
    • Role of reversible oxidation-reduction of enzyme thiols-disulfides in metabolic regulation
    • Ziegler D.M. Role of reversible oxidation-reduction of enzyme thiols-disulfides in metabolic regulation. Annu Rev Biochem 54 (1985) 305-329
    • (1985) Annu Rev Biochem , vol.54 , pp. 305-329
    • Ziegler, D.M.1
  • 24
    • 14844356880 scopus 로고    scopus 로고
    • Two Plasmodium falciparum ribonucleotide reductase small subunits, PfR2 and PfR4, interact with each other and are components of the in vivo enzyme complex
    • Bracchi-Ricard V., Moe D., and Chakrabarti D. Two Plasmodium falciparum ribonucleotide reductase small subunits, PfR2 and PfR4, interact with each other and are components of the in vivo enzyme complex. J Mol Biol 347 (2005) 749-758
    • (2005) J Mol Biol , vol.347 , pp. 749-758
    • Bracchi-Ricard, V.1    Moe, D.2    Chakrabarti, D.3
  • 25
  • 26
    • 0025260156 scopus 로고
    • Purines and pyrimidines in malarial parasites
    • Gero A.M., and O'Sullivan W.J. Purines and pyrimidines in malarial parasites. Blood Cells 16 (1990) 467-484
    • (1990) Blood Cells , vol.16 , pp. 467-484
    • Gero, A.M.1    O'Sullivan, W.J.2
  • 27
    • 33749515928 scopus 로고    scopus 로고
    • Regulation of apicomplexan microfilament dynamics by a minimal set of actin-binding proteins
    • Schüler H., and Matuschewski K. Regulation of apicomplexan microfilament dynamics by a minimal set of actin-binding proteins. Traffic 7 (2006) 1433-1439
    • (2006) Traffic , vol.7 , pp. 1433-1439
    • Schüler, H.1    Matuschewski, K.2
  • 31
    • 40549103113 scopus 로고    scopus 로고
    • 19 miniproteins can serve as targets for invasion inhibitory antibodies in Plasmodium falciparum provided they contain the correct domains for cell surface trafficking
    • 19 miniproteins can serve as targets for invasion inhibitory antibodies in Plasmodium falciparum provided they contain the correct domains for cell surface trafficking. Mol Microbiol 68 (2008) 124-138
    • (2008) Mol Microbiol , vol.68 , pp. 124-138
    • Gilson, P.R.1    O'Donnell, R.A.2    Nebl, T.3    Sanders, P.R.4    Wickham, M.E.5    McElwain, T.F.6
  • 33
    • 33846117155 scopus 로고    scopus 로고
    • A novel protein kinase family in Plasmodium falciparum is differentially transcribed and secreted to various cellular compartments of the host cell
    • Nunes C.M., Goldring J.P.D., Doerig C., and Scherf A. A novel protein kinase family in Plasmodium falciparum is differentially transcribed and secreted to various cellular compartments of the host cell. Mol Microbiol 63 (2007) 391-403
    • (2007) Mol Microbiol , vol.63 , pp. 391-403
    • Nunes, C.M.1    Goldring, J.P.D.2    Doerig, C.3    Scherf, A.4
  • 34
  • 35
    • 9144258616 scopus 로고    scopus 로고
    • Protein kinases of the human malaria parasite Plasmodium falciparum: the kinome of a divergent eukaryote
    • Ward P., Equinet L., Packer J., and Doerig C. Protein kinases of the human malaria parasite Plasmodium falciparum: the kinome of a divergent eukaryote. BMC Genomics 5 (2004) 79
    • (2004) BMC Genomics , vol.5 , pp. 79
    • Ward, P.1    Equinet, L.2    Packer, J.3    Doerig, C.4
  • 36
    • 0017311840 scopus 로고
    • Human malaria parasites in continuous culture
    • Trager W., and Jensen J.B. Human malaria parasites in continuous culture. Science 193 (1976) 673-675
    • (1976) Science , vol.193 , pp. 673-675
    • Trager, W.1    Jensen, J.B.2
  • 37
    • 17144413378 scopus 로고    scopus 로고
    • Roles of 1-Cys peroxiredoxin in haem detoxification in the human malaria parasite Plasmodium falciparum
    • Kawazu S., Ikenoue N., Takemae H., Komaki-Yasuda K., and Kano S. Roles of 1-Cys peroxiredoxin in haem detoxification in the human malaria parasite Plasmodium falciparum. FEBS J 272 (2005) 1784-1791
    • (2005) FEBS J , vol.272 , pp. 1784-1791
    • Kawazu, S.1    Ikenoue, N.2    Takemae, H.3    Komaki-Yasuda, K.4    Kano, S.5
  • 38
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227 (1970) 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.