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Volumn 148, Issue 2, 2006, Pages 144-160

Heterologous expression of proteins from Plasmodium falciparum: Results from 1000 genes

Author keywords

Cloning; E. coli; Insect cells; Ligase independent; Plasmodium falciparum; Protein expression; Structural genomics

Indexed keywords

6 PYRUVOYLTETRAHYDROPTERIN SYNTHASE; ADENOSINE DEAMINASE; ADENOSYLHOMOCYSTEINASE; ADENYLOSUCCINATE SYNTHASE; CHOLINE KINASE; CYCLOPHILIN; DEOXYURIDINE TRIPHOSPHATE PYROPHOSPHATASE; DNA TOPOISOMERASE; FERREDOXIN NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE REDUCTASE; GLYCERALDEHYDE 3 PHOSPHATE DEHYDROGENASE; GLYCEROL 3 PHOSPHATE DEHYDROGENASE; GLYCOGEN SYNTHASE KINASE; GUANOSINE TRIPHOSPHATASE; HELICASE; INITIATION FACTOR; INITIATION FACTOR 5A; LACTOYLGLUTATHIONE LYASE; METHIONINE ADENOSYLTRANSFERASE; NUCLEOSIDE DIPHOSPHATE KINASE; OROTIDINE 5' PHOSPHATE DECARBOXYLASE; PEPTIDASE; PHOSPHOGLYCERATE KINASE; PHOSPHOPROTEIN PHOSPHATASE; PROTEIN SERINE THREONINE KINASE; PROTOZOAL PROTEIN; RNA HELICASE; THIOREDOXIN; THIOREDOXIN REDUCTASE; UBIQUITIN CONJUGATING ENZYME; URIDINE PHOSPHORYLASE;

EID: 33745666810     PISSN: 01666851     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.molbiopara.2006.03.011     Document Type: Article
Times cited : (160)

References (62)
  • 1
    • 15044338866 scopus 로고    scopus 로고
    • The global distribution of clinical episodes of Plasmodium falciparum malaria
    • Snow R.W., Guerra C.A., Noor A.M., Myint H.Y., and Hay S.I. The global distribution of clinical episodes of Plasmodium falciparum malaria. Nature 434 7030 (2005) 214-217
    • (2005) Nature , vol.434 , Issue.7030 , pp. 214-217
    • Snow, R.W.1    Guerra, C.A.2    Noor, A.M.3    Myint, H.Y.4    Hay, S.I.5
  • 2
    • 33745650323 scopus 로고    scopus 로고
    • (2005). www.mmv.org
    • (2005)
  • 3
    • 14644417891 scopus 로고    scopus 로고
    • Optimized expression of Plasmodium falciparum erythrocyte membrane protein 1 domains in Escherichia coli
    • Flick K., Ahuja S., Chene A., Bejarano M.T., and Chen Q. Optimized expression of Plasmodium falciparum erythrocyte membrane protein 1 domains in Escherichia coli. Malar J 3 1 (2004) 50
    • (2004) Malar J , vol.3 , Issue.1 , pp. 50
    • Flick, K.1    Ahuja, S.2    Chene, A.3    Bejarano, M.T.4    Chen, Q.5
  • 4
    • 0034966663 scopus 로고    scopus 로고
    • Systematic optimization of expression and refolding of the Plasmodium falciparum cysteine protease falcipain-2
    • Sijwali P.S., Brinen L.S., and Rosenthal P.J. Systematic optimization of expression and refolding of the Plasmodium falciparum cysteine protease falcipain-2. Protein Expr Purif 22 1 (2001) 128-134
    • (2001) Protein Expr Purif , vol.22 , Issue.1 , pp. 128-134
    • Sijwali, P.S.1    Brinen, L.S.2    Rosenthal, P.J.3
  • 5
    • 7444220614 scopus 로고    scopus 로고
    • High-throughput generation of P. falciparum functional molecules by recombinational cloning
    • Aguiar J.C., LaBaer J., Blair P.L., et al. High-throughput generation of P. falciparum functional molecules by recombinational cloning. Genome Res 14 10B (2004) 2076-2082
    • (2004) Genome Res , vol.14 , Issue.10 B , pp. 2076-2082
    • Aguiar, J.C.1    LaBaer, J.2    Blair, P.L.3
  • 6
    • 0037015614 scopus 로고    scopus 로고
    • Genome sequence of the human malaria parasite Plasmodium falciparum
    • Gardner M.J., Hall N., Fung E., et al. Genome sequence of the human malaria parasite Plasmodium falciparum. Nature 419 6906 (2002) 498-511
    • (2002) Nature , vol.419 , Issue.6906 , pp. 498-511
    • Gardner, M.J.1    Hall, N.2    Fung, E.3
  • 7
    • 33745675197 scopus 로고    scopus 로고
    • www.nigms.nih.gov/psi/
  • 9
    • 14844294424 scopus 로고    scopus 로고
    • Protein production by auto-induction in high density shaking cultures
    • Studier F.W. Protein production by auto-induction in high density shaking cultures. Protein Expr Purif 41 1 (2005) 207-234
    • (2005) Protein Expr Purif , vol.41 , Issue.1 , pp. 207-234
    • Studier, F.W.1
  • 10
    • 10744233879 scopus 로고    scopus 로고
    • The TB structural genomics consortium: a resource for Mycobacterium tuberculosis biology
    • Terwilliger T.C., Park M.S., Waldo G.S., et al. The TB structural genomics consortium: a resource for Mycobacterium tuberculosis biology. Tuberculosis (Edinb) 83 4 (2003) 223-249
    • (2003) Tuberculosis (Edinb) , vol.83 , Issue.4 , pp. 223-249
    • Terwilliger, T.C.1    Park, M.S.2    Waldo, G.S.3
  • 11
    • 0033118395 scopus 로고    scopus 로고
    • Protein glycosylation in the malaria parasite
    • Gowda D.C., and Davidson E.A. Protein glycosylation in the malaria parasite. Parasitol Today 15 4 (1999) 147-152
    • (1999) Parasitol Today , vol.15 , Issue.4 , pp. 147-152
    • Gowda, D.C.1    Davidson, E.A.2
  • 12
    • 0347985825 scopus 로고    scopus 로고
    • Plasmodium biology: genomic gleanings
    • Aravind L., Iyer L.M., Wellems T.E., and Miller L.H. Plasmodium biology: genomic gleanings. Cell 115 7 (2003) 771-785
    • (2003) Cell , vol.115 , Issue.7 , pp. 771-785
    • Aravind, L.1    Iyer, L.M.2    Wellems, T.E.3    Miller, L.H.4
  • 13
    • 0035104190 scopus 로고    scopus 로고
    • Low-complexity regions in Plasmodium falciparum proteins
    • Pizzi E., and Frontali C. Low-complexity regions in Plasmodium falciparum proteins. Genome Res 11 2 (2001) 218-229
    • (2001) Genome Res , vol.11 , Issue.2 , pp. 218-229
    • Pizzi, E.1    Frontali, C.2
  • 14
    • 4644370187 scopus 로고    scopus 로고
    • Hyper-expansion of asparagines correlates with an abundance of proteins with prion-like domains in Plasmodium falciparum
    • Singh G.P., Chandra B.R., Bhattacharya A., Akhouri R.R., Singh S.K., and Sharma A. Hyper-expansion of asparagines correlates with an abundance of proteins with prion-like domains in Plasmodium falciparum. Mol Biochem Parasitol 137 2 (2004) 307-319
    • (2004) Mol Biochem Parasitol , vol.137 , Issue.2 , pp. 307-319
    • Singh, G.P.1    Chandra, B.R.2    Bhattacharya, A.3    Akhouri, R.R.4    Singh, S.K.5    Sharma, A.6
  • 15
    • 12344267747 scopus 로고    scopus 로고
    • Amino acid substitution and modification resulting from Escherichia coli expression of recombinant Plasmodium falciparum histidine-rich protein II
    • Schneider E.L., King D.S., and Marletta M.A. Amino acid substitution and modification resulting from Escherichia coli expression of recombinant Plasmodium falciparum histidine-rich protein II. Biochemistry 44 3 (2005) 987-995
    • (2005) Biochemistry , vol.44 , Issue.3 , pp. 987-995
    • Schneider, E.L.1    King, D.S.2    Marletta, M.A.3
  • 16
    • 0037134042 scopus 로고    scopus 로고
    • Divergent regulation of dihydrofolate reductase between malaria parasite and human host
    • Zhang K., and Rathod P.K. Divergent regulation of dihydrofolate reductase between malaria parasite and human host. Science 296 5567 (2002) 545-547
    • (2002) Science , vol.296 , Issue.5567 , pp. 545-547
    • Zhang, K.1    Rathod, P.K.2
  • 17
    • 0034951994 scopus 로고    scopus 로고
    • Over-production of lactate dehydrogenase from Plasmodium falciparum opens a new route to antimalarials
    • Turgut-Balik D., Shoemark D.K., Moreton K.M., Sessions R.B., and Holbrook J.J. Over-production of lactate dehydrogenase from Plasmodium falciparum opens a new route to antimalarials. Biotechnol Lett 23 (2001) 917-921
    • (2001) Biotechnol Lett , vol.23 , pp. 917-921
    • Turgut-Balik, D.1    Shoemark, D.K.2    Moreton, K.M.3    Sessions, R.B.4    Holbrook, J.J.5
  • 18
    • 0037246674 scopus 로고    scopus 로고
    • PlasmoDB: the Plasmodium genome resource. A database integrating experimental and computational data
    • Bahl A., Brunk B., Crabtree J., et al. PlasmoDB: the Plasmodium genome resource. A database integrating experimental and computational data. Nucleic Acids Res 31 1 (2003) 212-215
    • (2003) Nucleic Acids Res , vol.31 , Issue.1 , pp. 212-215
    • Bahl, A.1    Brunk, B.2    Crabtree, J.3
  • 19
    • 0037015621 scopus 로고    scopus 로고
    • The Plasmodium genome database
    • Kissinger J.C., Brunk B.P., Crabtree J., et al. The Plasmodium genome database. Nature 419 6906 (2002) 490-492
    • (2002) Nature , vol.419 , Issue.6906 , pp. 490-492
    • Kissinger, J.C.1    Brunk, B.P.2    Crabtree, J.3
  • 20
    • 0028501914 scopus 로고
    • Non-globular domains in protein sequences: automated segmentation using complexity measures
    • Wootton J.C. Non-globular domains in protein sequences: automated segmentation using complexity measures. Comput Chem 18 3 (1994) 269-285
    • (1994) Comput Chem , vol.18 , Issue.3 , pp. 269-285
    • Wootton, J.C.1
  • 22
    • 0020475449 scopus 로고
    • A simple method for displaying the hydropathic character of a protein
    • Kyte J., and Doolittle R.F. A simple method for displaying the hydropathic character of a protein. J Mol Biol 157 1 (1982) 105-132
    • (1982) J Mol Biol , vol.157 , Issue.1 , pp. 105-132
    • Kyte, J.1    Doolittle, R.F.2
  • 23
    • 9144261138 scopus 로고    scopus 로고
    • Mining the structural genomics pipeline: identification of protein properties that affect high-throughput experimental analysis
    • Goh C.S., Lan N., Douglas S.M., et al. Mining the structural genomics pipeline: identification of protein properties that affect high-throughput experimental analysis. J Mol Biol 336 1 (2004) 115-130
    • (2004) J Mol Biol , vol.336 , Issue.1 , pp. 115-130
    • Goh, C.S.1    Lan, N.2    Douglas, S.M.3
  • 24
    • 0023620327 scopus 로고
    • Codon usage in Plasmodium falciparum
    • Saul A., and Battistutta D. Codon usage in Plasmodium falciparum. Mol Biochem Parasitol 27 1 (1988) 35-42
    • (1988) Mol Biochem Parasitol , vol.27 , Issue.1 , pp. 35-42
    • Saul, A.1    Battistutta, D.2
  • 25
    • 33845488844 scopus 로고
    • AGA/AGG codon usage in parasites: implications for gene expression in Escherichia coli
    • Sayers J.R., Price H.P., Fallon P.G., and Doenhoff M.J. AGA/AGG codon usage in parasites: implications for gene expression in Escherichia coli. Parasitol Today 11 9 (1995) 345-346
    • (1995) Parasitol Today , vol.11 , Issue.9 , pp. 345-346
    • Sayers, J.R.1    Price, H.P.2    Fallon, P.G.3    Doenhoff, M.J.4
  • 26
    • 0033745103 scopus 로고    scopus 로고
    • Nucleotide bias causes a genomewide bias in the amino acid composition of proteins
    • Singer G.A., and Hickey D.A. Nucleotide bias causes a genomewide bias in the amino acid composition of proteins. Mol Biol Evol 17 11 (2000) 1581-1588
    • (2000) Mol Biol Evol , vol.17 , Issue.11 , pp. 1581-1588
    • Singer, G.A.1    Hickey, D.A.2
  • 27
    • 9144257886 scopus 로고    scopus 로고
    • The Pfam protein families database
    • Bateman A., Coin L., Durbin R., et al. The Pfam protein families database. Nucleic Acids Res 32 Database issue (2004) D138-D141
    • (2004) Nucleic Acids Res , vol.32 , Issue.Database issue
    • Bateman, A.1    Coin, L.2    Durbin, R.3
  • 28
    • 0037305599 scopus 로고    scopus 로고
    • Protein expression systems for structural genomics and proteomics
    • Yokoyama S. Protein expression systems for structural genomics and proteomics. Curr Opin Chem Biol 7 1 (2003) 39-43
    • (2003) Curr Opin Chem Biol , vol.7 , Issue.1 , pp. 39-43
    • Yokoyama, S.1
  • 29
    • 0034744173 scopus 로고    scopus 로고
    • Whole proteome pI values correlate with subcellular localizations of proteins for organisms within the three domains of life
    • Schwartz R., Ting C.S., and King J. Whole proteome pI values correlate with subcellular localizations of proteins for organisms within the three domains of life. Genome Res 11 5 (2001) 703-709
    • (2001) Genome Res , vol.11 , Issue.5 , pp. 703-709
    • Schwartz, R.1    Ting, C.S.2    King, J.3
  • 31
    • 0037466436 scopus 로고    scopus 로고
    • Low-complexity segments in Plasmodium falciparum proteins are primarily nucleic acid level adaptations
    • Xue H.Y., and Forsdyke D.R. Low-complexity segments in Plasmodium falciparum proteins are primarily nucleic acid level adaptations. Mol Biochem Parasitol 128 1 (2003) 21-32
    • (2003) Mol Biochem Parasitol , vol.128 , Issue.1 , pp. 21-32
    • Xue, H.Y.1    Forsdyke, D.R.2
  • 32
    • 0033999271 scopus 로고    scopus 로고
    • Overcoming codon bias: a method for high-level overexpression of Plasmodium and other AT-rich parasite genes in Escherichia coli
    • Baca A.M., and Hol W.G. Overcoming codon bias: a method for high-level overexpression of Plasmodium and other AT-rich parasite genes in Escherichia coli. Int J Parasitol 30 2 (2000) 113-118
    • (2000) Int J Parasitol , vol.30 , Issue.2 , pp. 113-118
    • Baca, A.M.1    Hol, W.G.2
  • 33
    • 0346850783 scopus 로고    scopus 로고
    • Codon optimization reveals critical factors for high level expression of two rare codon genes in Escherichia coli: RNA stability and secondary structure but not tRNA abundance
    • Wu X., Jornvall H., Berndt K.D., and Oppermann U. Codon optimization reveals critical factors for high level expression of two rare codon genes in Escherichia coli: RNA stability and secondary structure but not tRNA abundance. Biochem Biophys Res Commun 313 1 (2004) 89-96
    • (2004) Biochem Biophys Res Commun , vol.313 , Issue.1 , pp. 89-96
    • Wu, X.1    Jornvall, H.2    Berndt, K.D.3    Oppermann, U.4
  • 34
    • 0030566758 scopus 로고    scopus 로고
    • Chemical synthesis of the Plasmodium falciparum dihydrofolate reductase-thymidylate synthase gene
    • Prapunwattana P., Sirawaraporn W., Yuthavong Y., and Santi D.V. Chemical synthesis of the Plasmodium falciparum dihydrofolate reductase-thymidylate synthase gene. Mol Biochem Parasitol 83 1 (1996) 93-106
    • (1996) Mol Biochem Parasitol , vol.83 , Issue.1 , pp. 93-106
    • Prapunwattana, P.1    Sirawaraporn, W.2    Yuthavong, Y.3    Santi, D.V.4
  • 35
    • 0033557228 scopus 로고    scopus 로고
    • Vaccine candidate MSP-1 from Plasmodium falciparum: a redesigned 4917 bp polynucleotide enables synthesis and isolation of full-length protein from Escherichia coli and mammalian cells
    • Pan W., Ravot E., Tolle R., et al. Vaccine candidate MSP-1 from Plasmodium falciparum: a redesigned 4917 bp polynucleotide enables synthesis and isolation of full-length protein from Escherichia coli and mammalian cells. Nucleic Acids Res 27 4 (1999) 1094-1103
    • (1999) Nucleic Acids Res , vol.27 , Issue.4 , pp. 1094-1103
    • Pan, W.1    Ravot, E.2    Tolle, R.3
  • 36
    • 0037066782 scopus 로고    scopus 로고
    • Structural elucidation of the specificity of the antibacterial agent triclosan for malarial enoyl acyl carrier protein reductase
    • Perozzo R., Kuo M., Sidhu A.S., et al. Structural elucidation of the specificity of the antibacterial agent triclosan for malarial enoyl acyl carrier protein reductase. J Biol Chem 277 15 (2002) 13106-13114
    • (2002) J Biol Chem , vol.277 , Issue.15 , pp. 13106-13114
    • Perozzo, R.1    Kuo, M.2    Sidhu, A.S.3
  • 37
    • 0028804911 scopus 로고
    • Effects of rare codon clusters on high-level expression of heterologous proteins in Escherichia coli
    • Kane J.F. Effects of rare codon clusters on high-level expression of heterologous proteins in Escherichia coli. Curr Opin Biotechnol 6 5 (1995) 494-500
    • (1995) Curr Opin Biotechnol , vol.6 , Issue.5 , pp. 494-500
    • Kane, J.F.1
  • 38
    • 1442289362 scopus 로고    scopus 로고
    • Enhanced expression of a recombinant malaria candidate vaccine in Escherichia coli by codon optimization
    • Zhou Z., Schnake P., Xiao L., and Lal A.A. Enhanced expression of a recombinant malaria candidate vaccine in Escherichia coli by codon optimization. Protein Expr Purif 34 1 (2004) 87-94
    • (2004) Protein Expr Purif , vol.34 , Issue.1 , pp. 87-94
    • Zhou, Z.1    Schnake, P.2    Xiao, L.3    Lal, A.A.4
  • 39
    • 0042324336 scopus 로고    scopus 로고
    • Effect of codon optimization on expression levels of a functionally folded malaria vaccine candidate in prokaryotic and eukaryotic expression systems
    • Yadava A., and Ockenhouse C.F. Effect of codon optimization on expression levels of a functionally folded malaria vaccine candidate in prokaryotic and eukaryotic expression systems. Infect Immun 71 9 (2003) 4961-4969
    • (2003) Infect Immun , vol.71 , Issue.9 , pp. 4961-4969
    • Yadava, A.1    Ockenhouse, C.F.2
  • 40
    • 8544275816 scopus 로고    scopus 로고
    • Protein biophysical properties that correlate with crystallization success in Thermotoga maritima: maximum clustering strategy for structural genomics
    • Canaves J.M., Page R., Wilson I.A., and Stevens R.C. Protein biophysical properties that correlate with crystallization success in Thermotoga maritima: maximum clustering strategy for structural genomics. J Mol Biol 344 4 (2004) 977-991
    • (2004) J Mol Biol , vol.344 , Issue.4 , pp. 977-991
    • Canaves, J.M.1    Page, R.2    Wilson, I.A.3    Stevens, R.C.4
  • 41
    • 0033768266 scopus 로고    scopus 로고
    • Target selection for structural genomics
    • Brenner S.E. Target selection for structural genomics. Nat Struct Biol 7 Suppl. (2000) 967-969
    • (2000) Nat Struct Biol , vol.7 , Issue.SUPPL , pp. 967-969
    • Brenner, S.E.1
  • 42
    • 8044224013 scopus 로고    scopus 로고
    • Expression and characterisation of plasmepsin I from Plasmodium falciparum
    • Moon R.P., Tyas L., Certa U., et al. Expression and characterisation of plasmepsin I from Plasmodium falciparum. Eur J Biochem 244 2 (1997) 552-560
    • (1997) Eur J Biochem , vol.244 , Issue.2 , pp. 552-560
    • Moon, R.P.1    Tyas, L.2    Certa, U.3
  • 43
    • 0036451527 scopus 로고    scopus 로고
    • Utility of (His)6 tag for purification and refolding of proplasmepsin-2 and mutants with altered activation properties
    • Gulnik S.V., Afonina E.I., Gustchina E., et al. Utility of (His)6 tag for purification and refolding of proplasmepsin-2 and mutants with altered activation properties. Protein Expr Purif 24 3 (2002) 412-419
    • (2002) Protein Expr Purif , vol.24 , Issue.3 , pp. 412-419
    • Gulnik, S.V.1    Afonina, E.I.2    Gustchina, E.3
  • 44
    • 0031282471 scopus 로고    scopus 로고
    • Plasmodium falciparum: asparagine mutant at residue 108 of dihydrofolate reductase is an optimal antifolate-resistant single mutant
    • Sirawaraporn W., Yongkiettrakul S., Sirawaraporn R., Yuthavong Y., and Santi D.V. Plasmodium falciparum: asparagine mutant at residue 108 of dihydrofolate reductase is an optimal antifolate-resistant single mutant. Exp Parasitol 87 3 (1997) 245-252
    • (1997) Exp Parasitol , vol.87 , Issue.3 , pp. 245-252
    • Sirawaraporn, W.1    Yongkiettrakul, S.2    Sirawaraporn, R.3    Yuthavong, Y.4    Santi, D.V.5
  • 45
    • 22244460543 scopus 로고    scopus 로고
    • Improving expression and solubility of rice proteins produced as fusion proteins in Escherichia coli
    • Tsunoda Y., Sakai N., Kikuchi K., et al. Improving expression and solubility of rice proteins produced as fusion proteins in Escherichia coli. Protein Expr Purif 42 2 (2005) 268-277
    • (2005) Protein Expr Purif , vol.42 , Issue.2 , pp. 268-277
    • Tsunoda, Y.1    Sakai, N.2    Kikuchi, K.3
  • 46
    • 0347567036 scopus 로고    scopus 로고
    • Soluble expression of a functionally active Plasmodium falciparum falcipain-2 fused to maltose-binding protein in Escherichia coli
    • Goh L.L., Loke P., Singh M., and Sim T.S. Soluble expression of a functionally active Plasmodium falciparum falcipain-2 fused to maltose-binding protein in Escherichia coli. Protein Expr Purif 32 2 (2003) 194-201
    • (2003) Protein Expr Purif , vol.32 , Issue.2 , pp. 194-201
    • Goh, L.L.1    Loke, P.2    Singh, M.3    Sim, T.S.4
  • 47
    • 0042208063 scopus 로고    scopus 로고
    • Functional characterization of the propeptide of Plasmodium falciparum subtilisin-like protease-1
    • Jean L., Hackett F., Martin S.R., and Blackman M.J. Functional characterization of the propeptide of Plasmodium falciparum subtilisin-like protease-1. J Biol Chem 278 31 (2003) 28572-28579
    • (2003) J Biol Chem , vol.278 , Issue.31 , pp. 28572-28579
    • Jean, L.1    Hackett, F.2    Martin, S.R.3    Blackman, M.J.4
  • 48
    • 0037046096 scopus 로고    scopus 로고
    • Characterization of proteases involved in the processing of Plasmodium falciparum serine repeat antigen (SERA)
    • Li J., Matsuoka H., Mitamura T., and Horii T. Characterization of proteases involved in the processing of Plasmodium falciparum serine repeat antigen (SERA). Mol Biochem Parasitol 120 2 (2002) 177-186
    • (2002) Mol Biochem Parasitol , vol.120 , Issue.2 , pp. 177-186
    • Li, J.1    Matsuoka, H.2    Mitamura, T.3    Horii, T.4
  • 49
    • 0034900627 scopus 로고    scopus 로고
    • Factor A domain-related protein, a novel microneme protein of the malaria ookinete highly conserved throughout Plasmodium parasites
    • Yuda M., Yano K., Tsuboi T., Torii M., Chinzei Y., and von Willebrand. Factor A domain-related protein, a novel microneme protein of the malaria ookinete highly conserved throughout Plasmodium parasites. Mol Biochem Parasitol 116 1 (2001) 65-72
    • (2001) Mol Biochem Parasitol , vol.116 , Issue.1 , pp. 65-72
    • Yuda, M.1    Yano, K.2    Tsuboi, T.3    Torii, M.4    Chinzei, Y.5    von Willebrand6
  • 50
    • 0037147244 scopus 로고    scopus 로고
    • Analysis of the antimalarial drug resistance protein Pfcrt expressed in yeast
    • Zhang H., Howard E.M., and Roepe P.D. Analysis of the antimalarial drug resistance protein Pfcrt expressed in yeast. J Biol Chem 277 51 (2002) 49767-49775
    • (2002) J Biol Chem , vol.277 , Issue.51 , pp. 49767-49775
    • Zhang, H.1    Howard, E.M.2    Roepe, P.D.3
  • 51
    • 0035543204 scopus 로고    scopus 로고
    • High-level production and purification of P30P2MSP1(19), an important vaccine antigen for malaria, expressed in the methylotropic yeast Pichia pastoris
    • Brady C.P., Shimp R.L., Miles A.P., Whitmore M., and Stowers A.W. High-level production and purification of P30P2MSP1(19), an important vaccine antigen for malaria, expressed in the methylotropic yeast Pichia pastoris. Protein Expr Purif 23 3 (2001) 468-475
    • (2001) Protein Expr Purif , vol.23 , Issue.3 , pp. 468-475
    • Brady, C.P.1    Shimp, R.L.2    Miles, A.P.3    Whitmore, M.4    Stowers, A.W.5
  • 52
    • 0037039356 scopus 로고    scopus 로고
    • A recombinant vaccine expressed in the milk of transgenic mice protects Aotus monkeys from a lethal challenge with Plasmodium falciparum
    • Stowers A.W., Chen L.H., Zhang Y., et al. A recombinant vaccine expressed in the milk of transgenic mice protects Aotus monkeys from a lethal challenge with Plasmodium falciparum. Proc Natl Acad Sci USA 99 1 (2002) 339-344
    • (2002) Proc Natl Acad Sci USA , vol.99 , Issue.1 , pp. 339-344
    • Stowers, A.W.1    Chen, L.H.2    Zhang, Y.3
  • 53
    • 0242569192 scopus 로고    scopus 로고
    • Assistance of maltose binding protein to the in vivo folding of the disulfide-rich C-terminal fragment from Plasmodium falciparum merozoite surface protein 1 expressed in Escherichia coli
    • Planson A.G., Guijarro J.I., Goldberg M.E., and Chaffotte A.F. Assistance of maltose binding protein to the in vivo folding of the disulfide-rich C-terminal fragment from Plasmodium falciparum merozoite surface protein 1 expressed in Escherichia coli. Biochemistry 42 45 (2003) 13202-13211
    • (2003) Biochemistry , vol.42 , Issue.45 , pp. 13202-13211
    • Planson, A.G.1    Guijarro, J.I.2    Goldberg, M.E.3    Chaffotte, A.F.4
  • 54
    • 0036591274 scopus 로고    scopus 로고
    • Plasmodium falciparum: glycosylation status of Plasmodium falciparum circumsporozoite protein expressed in the baculovirus system
    • Kedees M.H., Azzouz N., Gerold P., et al. Plasmodium falciparum: glycosylation status of Plasmodium falciparum circumsporozoite protein expressed in the baculovirus system. Exp Parasitol 101 1 (2002) 64-68
    • (2002) Exp Parasitol , vol.101 , Issue.1 , pp. 64-68
    • Kedees, M.H.1    Azzouz, N.2    Gerold, P.3
  • 55
    • 7444250757 scopus 로고    scopus 로고
    • High-throughput expression of C. elegans proteins
    • Luan C.H., Qiu S., Finley J.B., et al. High-throughput expression of C. elegans proteins. Genome Res 14 10B (2004) 2102-2110
    • (2004) Genome Res , vol.14 , Issue.10 B , pp. 2102-2110
    • Luan, C.H.1    Qiu, S.2    Finley, J.B.3
  • 56
    • 14244271957 scopus 로고    scopus 로고
    • Parallel cloning, expression, purification and crystallization of human proteins for structural genomics
    • Ding H.T., Ren H., Chen Q., et al. Parallel cloning, expression, purification and crystallization of human proteins for structural genomics. Acta Crystallogr D Biol Crystallogr 58 Pt. 12 (2002) 2102-2108
    • (2002) Acta Crystallogr D Biol Crystallogr , vol.58 , Issue.PART 12 , pp. 2102-2108
    • Ding, H.T.1    Ren, H.2    Chen, Q.3
  • 57
    • 13244265563 scopus 로고    scopus 로고
    • Production of soluble mammalian proteins in Escherichia coli: identification of protein features that correlate with successful expression
    • Dyson M.R., Shadbolt S.P., Vincent K.J., Perera R.L., and McCafferty J. Production of soluble mammalian proteins in Escherichia coli: identification of protein features that correlate with successful expression. BMC Biotechnol 4 1 (2004) 32
    • (2004) BMC Biotechnol , vol.4 , Issue.1 , pp. 32
    • Dyson, M.R.1    Shadbolt, S.P.2    Vincent, K.J.3    Perera, R.L.4    McCafferty, J.5
  • 58
    • 0037022657 scopus 로고    scopus 로고
    • Proteome-scale purification of human proteins from bacteria
    • Braun P., Hu Y., Shen B., et al. Proteome-scale purification of human proteins from bacteria. Proc Natl Acad Sci USA 99 5 (2002) 2654-2659
    • (2002) Proc Natl Acad Sci USA , vol.99 , Issue.5 , pp. 2654-2659
    • Braun, P.1    Hu, Y.2    Shen, B.3
  • 59
    • 5644288963 scopus 로고    scopus 로고
    • A facile method for high-throughput co-expression of protein pairs
    • Alexandrov A., Vignali M., LaCount D.J., et al. A facile method for high-throughput co-expression of protein pairs. Mol Cell Proteomics 3 9 (2004) 934-938
    • (2004) Mol Cell Proteomics , vol.3 , Issue.9 , pp. 934-938
    • Alexandrov, A.1    Vignali, M.2    LaCount, D.J.3
  • 60
    • 0025085655 scopus 로고
    • Ligation-independent cloning of PCR products (LIC-PCR)
    • Aslanidis C., and de Jong P.J. Ligation-independent cloning of PCR products (LIC-PCR). Nucleic Acids Res 18 20 (1990) 6069-6074
    • (1990) Nucleic Acids Res , vol.18 , Issue.20 , pp. 6069-6074
    • Aslanidis, C.1    de Jong, P.J.2
  • 61
    • 3543064129 scopus 로고    scopus 로고
    • Cloning grills: high throughput cloning for structural genomics
    • Mehlin C., Boni E.E., Andreyka J., and Terry R.W. Cloning grills: high throughput cloning for structural genomics. J Struct Funct Genomics 5 1-2 (2004) 59-61
    • (2004) J Struct Funct Genomics , vol.5 , Issue.1-2 , pp. 59-61
    • Mehlin, C.1    Boni, E.E.2    Andreyka, J.3    Terry, R.W.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.