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Volumn 17, Issue 4, 2012, Pages 534-543

Insight into the selenoproteome of the malaria parasite Plasmodium falciparum

Author keywords

[No Author keywords available]

Indexed keywords

GREEN FLUORESCENT PROTEIN; PROTEIN PFSEL1; PROTEIN PFSEL4; PROTEIN SELK; PROTEIN SELT; SELENIUM; SELENOPROTEIN; UNCLASSIFIED DRUG;

EID: 84862563950     PISSN: 15230864     EISSN: 15577716     Source Type: Journal    
DOI: 10.1089/ars.2011.4276     Document Type: Article
Times cited : (15)

References (41)
  • 1
    • 3442876969 scopus 로고    scopus 로고
    • Normalization of real-time quantitative reverse transcription-PCR data: A model-based variance estimation approach to identify genes suited for normalization, applied to bladder and colon cancer data sets
    • DOI 10.1158/0008-5472.CAN-04-0496
    • Andersen CL, Jensen JL, and Orntoft TF. Normalization of real-time quantitative reverse transcription-PCR data: a model-based variance estimation approach to identify genes suited for normalization, applied to bladder and colon cancer data sets. Cancer Res 64: 5245-5250, 2004. (Pubitemid 39006544)
    • (2004) Cancer Research , vol.64 , Issue.15 , pp. 5245-5250
    • Andersen, C.L.1    Jensen, J.L.2    Orntoft, T.F.3
  • 4
    • 0027282772 scopus 로고
    • Functional characterization of the eukaryotic SECIS elements which direct selenocysteine insertion at UGA codons
    • Berry MJ, Banu L, Harney JW, and Larsen PR. Functional characterization of the eukaryotic SECIS elements which direct selenocysteine insertion at UGA codons. EMBO J 12: 3315-3322, 1993. (Pubitemid 23232763)
    • (1993) EMBO Journal , vol.12 , Issue.8 , pp. 3315-3322
    • Berry, M.J.1    Banu, L.2    Harney, J.W.3    Larsen, P.R.4
  • 5
    • 0026722791 scopus 로고
    • Substitution of cysteine for selenocysteine in type I iodothyronine deiodinase reduces the catalytic efficiency of the protein but enhances its translation
    • Berry MJ, Maia AL, Kieffer JD, Harney JW, and Larsen PR. Substitution of cysteine for selenocysteine in type I iodothyronine deiodinase reduces the catalytic efficiency of the protein but enhances its translation. Endocrinology 131: 1848-1852, 1992.
    • (1992) Endocrinology , vol.131 , pp. 1848-1852
    • Berry, M.J.1    Maia, A.L.2    Kieffer, J.D.3    Harney, J.W.4    Larsen, P.R.5
  • 6
    • 0033632277 scopus 로고    scopus 로고
    • Biosynthesis of selenoproteins - An overview
    • Bock A. Biosynthesis of selenoproteins - an overview. Biofactors 11: 77-78, 2000.
    • (2000) Biofactors , vol.11 , pp. 77-78
    • Bock, A.1
  • 7
    • 0034522027 scopus 로고    scopus 로고
    • The role of selenocysteine 133 in catalysis by the human type 2 iodothyronine deiodinase
    • DOI 10.1210/en.141.12.4606
    • Buettner C, Harney JW, and Larsen PR. The role of selenocysteine 133 in catalysis by the human type 2 iodothyronine deiodinase. Endocrinology 141: 4606-4612, 2000. (Pubitemid 32055139)
    • (2000) Endocrinology , vol.141 , Issue.12 , pp. 4606-4612
    • Buettner, C.1    Harney, J.W.2    Larsen, P.R.3
  • 8
    • 30744435823 scopus 로고    scopus 로고
    • Size matters: A view of selenocysteine incorporation from the ribosome
    • DOI 10.1007/s00018-005-5402-y
    • Caban K and Copeland PR. Size matters: a view of selenocysteine incorporation from the ribosome. Cell Mol Life Sci 63: 73-81, 2006. (Pubitemid 43100282)
    • (2006) Cellular and Molecular Life Sciences , vol.63 , Issue.1 , pp. 73-81
    • Caban, K.1    Copeland, P.R.2
  • 11
    • 0041317009 scopus 로고    scopus 로고
    • Mechanism and regulation of selenoprotein synthesis
    • DOI 10.1146/annurev.nutr.23.011702.073318
    • Driscoll DM and Copeland PR. Mechanism and regulation of selenoprotein synthesis. Annu Rev Nutr 23: 17-40, 2003. (Pubitemid 37059714)
    • (2003) Annual Review of Nutrition , vol.23 , pp. 17-40
    • Driscoll, D.M.1    Copeland, P.R.2
  • 12
    • 7244240741 scopus 로고    scopus 로고
    • Modified fixed-ratio isobologram method for studying in vitro interactions between atovaquone and proguanil or dihydroartemisinin against drug-resistant strains of Plasmodium falciparum
    • DOI 10.1128/AAC.48.11.4097-4102.2004
    • Fivelman QL, Adagu IS, and Warhurst DC. Modified fixedratio isobologram method for studying in vitro interactions between atovaquone and proguanil or dihydroartemisinin against drug-resistant strains of Plasmodium falciparum. Antimicrob Agents Chemother 48: 4097-4102, 2004. (Pubitemid 39434861)
    • (2004) Antimicrobial Agents and Chemotherapy , vol.48 , Issue.11 , pp. 4097-4102
    • Fivelman, Q.L.1    Adagu, I.S.2    Warhurst, D.C.3
  • 14
    • 77951938957 scopus 로고    scopus 로고
    • Regulation of redox signaling by selenoproteins
    • Hawkes WC and Alkan Z. Regulation of redox signaling by selenoproteins. Biol Trace Elem Res 134: 235-251, 2010.
    • (2010) Biol Trace Elem Res , vol.134 , pp. 235-251
    • Hawkes, W.C.1    Alkan, Z.2
  • 16
    • 0025056591 scopus 로고
    • Evidence that UGA is read as a tryptophan codon rather than as a stop codon by Mycoplasma pneumoniae, Mycoplasma genitalium, and Mycoplasma gallisepticum
    • Inamine JM, Ho KC, Loechel S, and Hu PC. Evidence that UGAis read as a tryptophan codon rather than as a stop codon by Mycoplasma pneumoniae, Mycoplasma genitalium, and Mycoplasma gallisepticum. J Bacteriol 172: 504-506, 1990. (Pubitemid 20016876)
    • (1990) Journal of Bacteriology , vol.172 , Issue.1 , pp. 504-506
    • Inamine, J.M.1    Ho, K.-C.2    Loechel, S.3    Hu, P.-C.4
  • 17
    • 79957693495 scopus 로고    scopus 로고
    • Glucose-6-phosphate dehydrogenase-6-phosphogluconolactonase: A unique bifunctional enzyme from Plasmodium falciparum
    • Jortzik E, Mailu BM, Preuss J, Fischer M, Bode L, Rahlfs S, and Becker K. Glucose-6-phosphate dehydrogenase-6-phosphogluconolactonase: a unique bifunctional enzyme from Plasmodium falciparum. Biochem J 436: 641-650, 2011.
    • (2011) Biochem J , vol.436 , pp. 641-650
    • Jortzik, E.1    Mailu, B.M.2    Preuss, J.3    Fischer, M.4    Bode, L.5    Rahlfs, S.6    Becker, K.7
  • 18
    • 70450250730 scopus 로고    scopus 로고
    • FastPCR software for PCR primer and probe design and repeat search
    • Kalendar R, Lee D, and Schulman AH. FastPCR software for PCR primer and probe design and repeat search. Genes, Genomes and Genomics 3: 1-14, 2009.
    • (2009) Genes, Genomes and Genomics , vol.3 , pp. 1-14
    • Kalendar, R.1    Lee, D.2    Schulman, A.H.3
  • 19
    • 0023929362 scopus 로고
    • The isolation and purification of a specific "protector" protein which inhibits enzyme inactivation by a thiol/Fe(III)/O2 mixedfunction oxidation system
    • Kim K, Kim IH, Lee KY, Rhee SG, and Stadtman ER. The isolation and purification of a specific "protector" protein which inhibits enzyme inactivation by a thiol/Fe(III)/O2 mixedfunction oxidation system. J Biol Chem263: 4704-4711, 1988.
    • (1988) J Biol Chem , vol.263 , pp. 4704-4711
    • Kim, K.1    Kim, I.H.2    Lee, K.Y.3    Rhee, S.G.4    Stadtman, E.R.5
  • 22
    • 33845877955 scopus 로고    scopus 로고
    • Hypervariability within the Rifin, Stevor and Pfmc-2TM superfamilies in plasmodium falciparum
    • DOI 10.1093/nar/gkl942
    • Lavazec C, Sanyal S, and Templeton TJ. Hypervariability within the Rifin, Stevor and Pfmc-2TM superfamilies in Plasmodium falciparum. Nucleic Acids Res 34: 6696-6707, 2006. (Pubitemid 46017961)
    • (2006) Nucleic Acids Research , vol.34 , Issue.22 , pp. 6696-6707
    • Lavazec, C.1    Sanyal, S.2    Templeton, T.J.3
  • 23
    • 0023087564 scopus 로고
    • A global view of human selenium nutrition
    • Levander OA. A global view of human selenium nutrition. Annu Rev Nutr 7: 227-250, 1987.
    • (1987) Annu Rev Nutr , vol.7 , pp. 227-250
    • Levander, O.A.1
  • 24
    • 0031892227 scopus 로고    scopus 로고
    • Different seleniumcontaining proteins in the extracellular and intracellular media of leucocytes cultivated in vitro
    • Liu Q, Lauridsen E, and Clausen J. Different seleniumcontaining proteins in the extracellular and intracellular media of leucocytes cultivated in vitro. Biol Trace Elem Res 61: 237-252, 1998.
    • (1998) Biol Trace Elem Res , vol.61 , pp. 237-252
    • Liu, Q.1    Lauridsen, E.2    Clausen, J.3
  • 26
    • 33748919323 scopus 로고    scopus 로고
    • Identification and characterization of selenoprotein K: An antioxidant in cardiomyocytes
    • DOI 10.1016/j.febslet.2006.08.065, PII S0014579306010283
    • Lu C, Qiu F, Zhou H, Peng Y, Hao W, Xu J, Yuan J, Wang S, Qiang B, Xu C, and Peng X. Identification and characterization of selenoprotein K: an antioxidant in cardiomyocytes. FEBS Lett 580: 5189-5197, 2006. (Pubitemid 44430096)
    • (2006) FEBS Letters , vol.580 , Issue.22 , pp. 5189-5197
    • Lu, C.1    Qiu, F.2    Zhou, H.3    Peng, Y.4    Hao, W.5    Xu, J.6    Yuan, J.7    Wang, S.8    Qiang, B.9    Xu, C.10    Peng, X.11
  • 28
  • 29
    • 17344392308 scopus 로고    scopus 로고
    • A new mathematical model for relative quantification in real-time RT-PCR
    • Pfaffl MW. A new mathematical model for relative quantification in real-time RT-PCR. Nucleic Acids Res 29: e45, 2001.
    • (2001) Nucleic Acids Res , vol.29
    • Pfaffl, M.W.1
  • 30
    • 80855138132 scopus 로고    scopus 로고
    • Thioredoxin-glutathione reductase: Its role in redox biology and potential as a target for drugs against neglected diseases
    • Prast-Nielsen S, Huang HH, and Williams DL. Thioredoxin-glutathione reductase: Its role in redox biology and potential as a target for drugs against neglected diseases. Biochim Biophys Acta 1810: 1262-1271, 2011.
    • (2011) Biochim Biophys Acta , vol.1810 , pp. 1262-1271
    • Prast-Nielsen, S.1    Huang, H.H.2    Williams, D.L.3
  • 31
    • 67650805623 scopus 로고    scopus 로고
    • The human selenoproteome: Recent insights into functions and regulation
    • Reeves MA and Hoffmann PR. The human selenoproteome: recent insights into functions and regulation. Cell Mol Life Sci 66: 2457-2478, 2009.
    • (2009) Cell Mol Life Sci , vol.66 , pp. 2457-2478
    • Reeves, M.A.1    Hoffmann, P.R.2
  • 32
    • 73049095378 scopus 로고    scopus 로고
    • Hierarchical regulation of selenoprotein expression and sex-specific effects of selenium
    • Schomburg L and Schweizer U. Hierarchical regulation of selenoprotein expression and sex-specific effects of selenium. Biochim Biophys Acta 1790: 1453-1462, 2009.
    • (2009) Biochim Biophys Acta , vol.1790 , pp. 1453-1462
    • Schomburg, L.1    Schweizer, U.2
  • 34
    • 72649088108 scopus 로고    scopus 로고
    • Transcriptional regulation of mammalian selenoprotein expression
    • Stoytcheva ZR and Berry MJ. Transcriptional regulation of mammalian selenoprotein expression. Biochim Biophys Acta 1790: 1429-1440, 2009.
    • (2009) Biochim Biophys Acta , vol.1790 , pp. 1429-1440
    • Stoytcheva, Z.R.1    Berry, M.J.2
  • 37
    • 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
    • DOI 10.1016/j.molbiopara.2004.05.009, PII S0166685104001525
    • Tonkin CJ, van Dooren GG, Spurck TP, Struck NS, Good RT, Handman E, Cowman AF, and McFadden GI. 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. (Pubitemid 38987938)
    • (2004) Molecular and Biochemical Parasitology , vol.137 , Issue.1 , pp. 13-21
    • Tonkin, C.J.1    Van Dooren, G.G.2    Spurck, T.P.3    Struck, N.S.4    Good, R.T.5    Handman, E.6    Cowman, A.F.7    McFadden, G.I.8
  • 39
    • 0037129827 scopus 로고    scopus 로고
    • Accurate normalization of real-time quantitative RT-PCR data by geometric averaging of multiple internal control genes
    • Vandesompele J, De Preter K, Pattyn F, Poppe B, Van Roy N, De Paepe A, and Speleman F. Accurate normalization of real-time quantitative RT-PCR data by geometric averaging of multiple internal control genes. Genome Biol 3: RESEARCH0034, 2002.
    • (2002) Genome Biol , vol.3
    • Vandesompele, J.1    De Preter, K.2    Pattyn, F.3    Poppe, B.4    Van Roy, N.5    De Paepe, A.6    Speleman, F.7
  • 40
    • 79952193925 scopus 로고    scopus 로고
    • Available at Accessed on October 12, 2011
    • WHO. World Malaria Report 2010. Available at www.who .int/malaria/world- malaria-report-2010/worldmalariareport 2010.pdf. 2010 Accessed on October 12, 2011.
    • (2010) World Malaria Report 2010
  • 41
    • 0034674566 scopus 로고    scopus 로고
    • Essential role of selenium in the catalytic activities of mammalian thioredoxin reductase revealed by characterization of recombinant enzymes with selenocysteine mutations
    • DOI 10.1074/jbc.M000690200
    • Zhong L and Holmgren A. Essential role of selenium in the catalytic activities of mammalian thioredoxin reductase revealed by characterization of recombinant enzymes with selenocysteine mutations. J Biol Chem 275: 18121-18128, 2000. (Pubitemid 30414762)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.24 , pp. 18121-18128
    • Zhong, L.1    Holmgren, A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.