메뉴 건너뛰기




Volumn 896, Issue , 2016, Pages 199-215

The multibac baculovirus/insect cell expression vector system for producing complex protein biologics

Author keywords

Baculovirus; Electron microscopy; Gene transfer; Insect cell expression system; Lepidoptera; MultiBac; Protein complexes; Structural biology; Synthetic biology; Vaccines; Virus like particles (VLPs); X ray crystallography

Indexed keywords

CHIKUNGUNYA VACCINE; GLYCOPROTEIN; INFLUENZA VACCINE; MULTIPROTEIN COMPLEX; POLYPROTEIN; UNCLASSIFIED DRUG; VIRUS VACCINE; PROTEIN SUBUNIT; RECOMBINANT PROTEIN; VIRAL PROTEIN;

EID: 84978976585     PISSN: 00652598     EISSN: 22148019     Source Type: Book Series    
DOI: 10.1007/978-3-319-27216-0_13     Document Type: Chapter
Times cited : (65)

References (84)
  • 1
    • 0021010433 scopus 로고
    • Production of human beta interferon in insect cells infected with a baculovirus expression vector
    • Smith GE, Summers MD, Fraser MJ (1983) Production of human beta interferon in insect cells infected with a baculovirus expression vector. Mol Cell Biol 3:2156–2165
    • (1983) Mol Cell Biol , vol.3 , pp. 2156-2165
    • Smith, G.E.1    Summers, M.D.2    Fraser, M.J.3
  • 2
    • 33748753155 scopus 로고    scopus 로고
    • Milestones leading to the genetic engineering of baculoviruses as expression vector systems and viral pesticides
    • Summers MD (2006) Milestones leading to the genetic engineering of baculoviruses as expression vector systems and viral pesticides. Adv Virus Res 68:3–73
    • (2006) Adv Virus Res , vol.68 , pp. 3-73
    • Summers, M.D.1
  • 3
    • 0021401669 scopus 로고
    • Strong and regulated expression of Escherichia coli betagalactosidase in insect cells with a baculoviral vector
    • Pennock GD, Shoemaker C, Miller LK (1984) Strong and regulated expression of Escherichia coli betagalactosidase in insect cells with a baculoviral vector. Mol Cell Biol 4:399–406
    • (1984) Mol Cell Biol , vol.4 , pp. 399-406
    • Pennock, G.D.1    Shoemaker, C.2    Miller, L.K.3
  • 4
    • 84918829335 scopus 로고    scopus 로고
    • Thirty years of baculovirus-insect cell protein expression: From dark horse to mainstream technology
    • van Oers MM, Plijman GP, Vlak JM (2015) Thirty years of baculovirus-insect cell protein expression: from dark horse to mainstream technology. J Gen Virol 96:6–23
    • (2015) J Gen Virol , vol.96 , pp. 6-23
    • Van Oers, M.M.1    Plijman, G.P.2    Vlak, J.M.3
  • 6
    • 71549150895 scopus 로고    scopus 로고
    • Baculovirus-insect cell expression systems
    • Jarvis DL (2009) Baculovirus-insect cell expression systems. Methods Enzymol 463:191–222
    • (2009) Methods Enzymol , vol.463 , pp. 191-222
    • Jarvis, D.L.1
  • 7
    • 36048968091 scopus 로고    scopus 로고
    • Baculovirus transfer vectors
    • Possee RD, King LA (2007) Baculovirus transfer vectors. Methods Mol Biol 388:55–76
    • (2007) Methods Mol Biol , vol.388 , pp. 55-76
    • Possee, R.D.1    King, L.A.2
  • 8
    • 80054845228 scopus 로고    scopus 로고
    • Characterisation of protection afforded by a bivaleent virus-like partcile vaccine against bluetongue virus serotypes 1 and 4 in sheep
    • Perez de Diego AC et al (2011) Characterisation of protection afforded by a bivaleent virus-like partcile vaccine against bluetongue virus serotypes 1 and 4 in sheep. PLoS One 6:e26666
    • (2011) Plos One , vol.6
    • Perez De Diego, A.C.1
  • 11
    • 77955255595 scopus 로고    scopus 로고
    • Virus-like partciles as a vaccine delivery system: Myths and facts
    • Roy P, Noad R (2009) Virus-like partciles as a vaccine delivery system: myths and facts. Adv Exp Med Biol 655:145–158
    • (2009) Adv Exp Med Biol , vol.655 , pp. 145-158
    • Roy, P.1    Noad, R.2
  • 12
    • 84896368264 scopus 로고    scopus 로고
    • OneBac: Platform for scalable and high-titer production of adeno-associated virus serotype 1–12 vectors for gene therapy
    • Mietzsch M et al (2014) OneBac: platform for scalable and high-titer production of adeno-associated virus serotype 1–12 vectors for gene therapy. Hum Gene Ther 25(3):212–222
    • (2014) Hum Gene Ther , vol.25 , Issue.3 , pp. 212-222
    • Mietzsch, M.1
  • 13
    • 84905891143 scopus 로고    scopus 로고
    • Vector design Tour de Force: Integrating combinatorial and rational approaches to derive novel adeno-associated virus variants
    • Marsic D et al (2014) Vector design Tour de Force: integrating combinatorial and rational approaches to derive novel adeno-associated virus variants. Mol Ther 22(11):1900–1909
    • (2014) Mol Ther , vol.22 , Issue.11 , pp. 1900-1909
    • Marsic, D.1
  • 14
    • 79956006654 scopus 로고    scopus 로고
    • Large-scale recombinant adenoassociated virus production
    • Kotin RM (2011) Large-scale recombinant adenoassociated virus production. Hum Mol Genet 20(R1):R2–R6
    • (2011) Hum Mol Genet , vol.20 , Issue.1
    • Kotin, R.M.1
  • 15
    • 84878549291 scopus 로고    scopus 로고
    • Baculovirus: An insect- derived vector for diverse gene transfer applications
    • Airenne KJ et al (2013) Baculovirus: an insect- derived vector for diverse gene transfer applications. Mol Ther 21(4):739–749
    • (2013) Mol Ther , vol.21 , Issue.4 , pp. 739-749
    • Airenne, K.J.1
  • 16
    • 84901459154 scopus 로고    scopus 로고
    • Bioengineered baculoviruses as new class of therapeutics using micro and nanotechnologies: Principles, prospects and challenges
    • Paul A, Hasan A, Rodes L, Sangaralingam M, Prakash S (2014) Bioengineered baculoviruses as new class of therapeutics using micro and nanotechnologies: principles, prospects and challenges. Adv Drug Deliv Rev 71:115–130
    • (2014) Adv Drug Deliv Rev , vol.71 , pp. 115-130
    • Paul, A.1    Hasan, A.2    Rodes, L.3    Sangaralingam, M.4    Prakash, S.5
  • 17
    • 11144340226 scopus 로고    scopus 로고
    • Baculovirus expression system for heterologous multiprotein complexes
    • Berger I, Fitzgerald DJ, Richmond TJ (2004) Baculovirus expression system for heterologous multiprotein complexes. Nat Biotechnol 22(12):1583–1587
    • (2004) Nat Biotechnol , vol.22 , Issue.12 , pp. 1583-1587
    • Berger, I.1    Fitzgerald, D.J.2    Richmond, T.J.3
  • 18
    • 33751247668 scopus 로고    scopus 로고
    • Protein complex expression by using multigene baculoviral vectors
    • Fitzgerald DJ et al (2006) Protein complex expression by using multigene baculoviral vectors. Nat Methods 3(12):1021–1032
    • (2006) Nat Methods , vol.3 , Issue.12 , pp. 1021-1032
    • Fitzgerald, D.J.1
  • 19
    • 33847661963 scopus 로고    scopus 로고
    • Multiprotein expression strategy for structural biology of eukaryotic complexes
    • Fitzgerald DJ et al (2007) Multiprotein expression strategy for structural biology of eukaryotic complexes. Structure 15(3):275–279
    • (2007) Structure , vol.15 , Issue.3 , pp. 275-279
    • Fitzgerald, D.J.1
  • 20
    • 60849095081 scopus 로고    scopus 로고
    • Towards eukaryotic structural complexomics
    • Bieniossek C, Berger I (2009) Towards eukaryotic structural complexomics. J Struct Funct Genomics 10(1):37–46
    • (2009) J Struct Funct Genomics , vol.10 , Issue.1 , pp. 37-46
    • Bieniossek, C.1    Berger, I.2
  • 21
    • 77955962894 scopus 로고    scopus 로고
    • New baculovirus expression tools for recombinant protein complex production
    • Trowitzsch S, Bieniossek C, Nie Y, Garzoni F, Berger I (2010) New baculovirus expression tools for recombinant protein complex production. J Struct Biol 172(1):45–54
    • (2010) J Struct Biol , vol.172 , Issue.1 , pp. 45-54
    • Trowitzsch, S.1    Bieniossek, C.2    Nie, Y.3    Garzoni, F.4    Berger, I.5
  • 22
    • 79960027830 scopus 로고    scopus 로고
    • Robots, pipelines, polyproteins: Enabling multiprotein expression in prokaryotic and eukaryotic cells
    • Vijayachandran LS et al (2011) Robots, pipelines, polyproteins: enabling multiprotein expression in prokaryotic and eukaryotic cells. J Struct Biol 175(2):198–208
    • (2011) J Struct Biol , vol.175 , Issue.2 , pp. 198-208
    • Vijayachandran, L.S.1
  • 24
    • 84880146698 scopus 로고    scopus 로고
    • The MultiBac protein complex production platform at the EMBL
    • Berger I et al (2013) The MultiBac protein complex production platform at the EMBL. J Vis Exp 11(77):e50159
    • (2013) J Vis Exp , vol.11 , Issue.77
    • Berger, I.1
  • 25
    • 84884389156 scopus 로고    scopus 로고
    • High-throughput screening of multiple protein complexes
    • Berger I, Chaillet M, Garzoni F, Yau-Rose S, Zoro B (2013) High-throughput screening of multiple protein complexes. Am Lab 25(8):32–35
    • (2013) Am Lab , vol.25 , Issue.8 , pp. 32-35
    • Berger, I.1    Chaillet, M.2    Garzoni, F.3    Yau-Rose, S.4    Zoro, B.5
  • 26
    • 73349084591 scopus 로고    scopus 로고
    • Getting a grip on complexes
    • Nie Y et al (2009) Getting a grip on complexes. Curr Genomics 10(8):558–572
    • (2009) Curr Genomics , vol.10 , Issue.8 , pp. 558-572
    • Nie, Y.1
  • 27
    • 37249065351 scopus 로고    scopus 로고
    • The molecular sociology of the cell
    • Robinson CV, Sali A, Baumeister W (2007) The molecular sociology of the cell. Nature 450(7172):973–982
    • (2007) Nature , vol.450 , Issue.7172 , pp. 973-982
    • Robinson, C.V.1    Sali, A.2    Baumeister, W.3
  • 28
    • 84911474165 scopus 로고    scopus 로고
    • The ribosome emerges from a black box
    • Ramakrishnan V (2014) The ribosome emerges from a black box. Cell 159(5):979–984
    • (2014) Cell , vol.159 , Issue.5 , pp. 979-984
    • Ramakrishnan, V.1
  • 29
    • 84886947664 scopus 로고    scopus 로고
    • Crystal structure of the 14-subunit RNA polymerase I
    • Fernández-Tornero C et al (2013) Crystal structure of the 14-subunit RNA polymerase I. Nature 502(7473):644–649
    • (2013) Nature , vol.502 , Issue.7473 , pp. 644-649
    • Fernández-Tornero, C.1
  • 30
    • 84886948058 scopus 로고    scopus 로고
    • RNA polymerase I structure and transcription regulation
    • Engel C, Sainsbury S, Cheung AC, Kostrewa D, Cramer P (2013) RNA polymerase I structure and transcription regulation. Nature 502(7473):650–655
    • (2013) Nature , vol.502 , Issue.7473 , pp. 650-655
    • Engel, C.1    Sainsbury, S.2    Cheung, A.C.3    Kostrewa, D.4    Cramer, P.5
  • 31
    • 48249103199 scopus 로고    scopus 로고
    • Structure of eukaryotic RNA polymerases
    • Cramer P et al (2008) Structure of eukaryotic RNA polymerases. Annu Rev Biophys 37:337–352
    • (2008) Annu Rev Biophys , vol.37 , pp. 337-352
    • Cramer, P.1
  • 32
    • 77955930508 scopus 로고    scopus 로고
    • Interaction proteomics: Characterization of protein complexes using tandem affinity purification-mass spectrometry
    • Völkel P, Le Faou P, Angrand PO (2010) Interaction proteomics: characterization of protein complexes using tandem affinity purification-mass spectrometry. Biochem Soc Trans 38(4):883–887
    • (2010) Biochem Soc Trans , vol.38 , Issue.4 , pp. 883-887
    • Völkel, P.1    Le Faou, P.2    Angrand, P.O.3
  • 33
    • 77954821990 scopus 로고    scopus 로고
    • Commonly used tag combinations for tandem affinity purification
    • Li Y (2010) Commonly used tag combinations for tandem affinity purification. Biotechnol Appl Biochem 55(2):73–83
    • (2010) Biotechnol Appl Biochem , vol.55 , Issue.2 , pp. 73-83
    • Li, Y.1
  • 34
    • 0038169958 scopus 로고    scopus 로고
    • Genome-wide studies of protein-protein interaction
    • Janin J, Séraphin B (2003) Genome-wide studies of protein-protein interaction. Curr Opin Struct Biol 13(3):383–388
    • (2003) Curr Opin Struct Biol , vol.13 , Issue.3 , pp. 383-388
    • Janin, J.1    Séraphin, B.2
  • 35
    • 84879185251 scopus 로고    scopus 로고
    • Protein production from the structural genomics perspective: Achievements and future needs
    • Almo SC et al (2013) Protein production from the structural genomics perspective: achievements and future needs. Curr Opin Struct Biol 23(3):335–344
    • (2013) Curr Opin Struct Biol , vol.23 , Issue.3 , pp. 335-344
    • Almo, S.C.1
  • 36
    • 84918837387 scopus 로고    scopus 로고
    • Characterization and production of protein complexes by co-expression in Escherichia coli
    • Haffke M et al (2015) Characterization and production of protein complexes by co-expression in Escherichia coli. Methods Mol Biol 1261:63–89
    • (2015) Methods Mol Biol , vol.1261 , pp. 63-89
    • Haffke, M.1
  • 37
    • 84879147807 scopus 로고    scopus 로고
    • Expression in Escherichia coli: Becoming faster and more complex
    • Vincentelli R, Romier C (2013) Expression in Escherichia coli: becoming faster and more complex. Curr Opin Struct Biol 23(3):326–334
    • (2013) Curr Opin Struct Biol , vol.23 , Issue.3 , pp. 326-334
    • Vincentelli, R.1    Romier, C.2
  • 38
    • 67349278136 scopus 로고    scopus 로고
    • Automated unrestricted multigene recombineering for multiprotein complex production
    • Bieniossek C et al (2009) Automated unrestricted multigene recombineering for multiprotein complex production. Nat Methods 6(6):447–450
    • (2009) Nat Methods , vol.6 , Issue.6 , pp. 447-450
    • Bieniossek, C.1
  • 39
    • 84954601111 scopus 로고    scopus 로고
    • The production of multiprotein complexes in insect cells using the baculovirus expression system
    • Abdulrahman W et al (2015) The production of multiprotein complexes in insect cells using the baculovirus expression system. Methods Mol Biol 1261:91–114
    • (2015) Methods Mol Biol , vol.1261 , pp. 91-114
    • Abdulrahman, W.1
  • 40
    • 84856690548 scopus 로고    scopus 로고
    • MultiBac: Expanding the research toolbox for multiprotein complexes
    • Bieniossek C, Imasaki T, Takagi Y, Berger I (2012) MultiBac: expanding the research toolbox for multiprotein complexes. Trends Biochem Sci 37(2):49–57
    • (2012) Trends Biochem Sci , vol.37 , Issue.2 , pp. 49-57
    • Bieniossek, C.1    Imasaki, T.2    Takagi, Y.3    Berger, I.4
  • 42
    • 0019869802 scopus 로고
    • Replication control and switch-off function as observed with a mini-F factor plasmid
    • Tsutsui H, Matsubara K (1981) Replication control and switch-off function as observed with a mini-F factor plasmid. J Bacteriol 147(2):509–516
    • (1981) J Bacteriol , vol.147 , Issue.2 , pp. 509-516
    • Tsutsui, H.1    Matsubara, K.2
  • 43
    • 0027209690 scopus 로고
    • Efficient generation of infectious recombinant baculoviruses by site-specific transposon-mediated insertion of foreign genes into a baculovirus genome propagated in Escherichia coli
    • Luckow VA, Lee SC, Barry GF, Olins PO (1993) Efficient generation of infectious recombinant baculoviruses by site-specific transposon-mediated insertion of foreign genes into a baculovirus genome propagated in Escherichia coli. J Virol 67:4566–4579
    • (1993) J Virol , vol.67 , pp. 4566-4579
    • Luckow, V.A.1    Lee, S.C.2    Barry, G.F.3    Olins, P.O.4
  • 44
    • 84859237513 scopus 로고    scopus 로고
    • SweetBac: A new approach for the production of mammalianised glycoproteins in insect cells
    • Palmberger D, Wilson IB, Berger I, Grabherr R, Rendic D (2012) SweetBac: a new approach for the production of mammalianised glycoproteins in insect cells. PLoS One 7(4):e34226
    • (2012) Plos One , vol.7 , Issue.4
    • Palmberger, D.1    Wilson, I.B.2    Berger, I.3    Grabherr, R.4    Rendic, D.5
  • 46
    • 84906948184 scopus 로고    scopus 로고
    • Minimizing fucosylation in insect cell-derived glycoproteins reduces binding to IgE antibodies from the sera of patients with allergy
    • Palmberger D et al (2014) Minimizing fucosylation in insect cell-derived glycoproteins reduces binding to IgE antibodies from the sera of patients with allergy. Biotechnol J 9(SI):1206–1214
    • (2014) Biotechnol J , vol.9 , pp. 1206-1214
    • Palmberger, D.1
  • 47
    • 61749088744 scopus 로고    scopus 로고
    • The titerless infected-cells preservation and scale-up (TIPS) method for largescale production of NO-sensitive human soluble guanylate cyclase (sGC) from insect cells infected with recombinant baculovirus
    • Wasilko DJ et al (2009) The titerless infected-cells preservation and scale-up (TIPS) method for largescale production of NO-sensitive human soluble guanylate cyclase (sGC) from insect cells infected with recombinant baculovirus. Protein Expr Purif 65(2):122–132
    • (2009) Protein Expr Purif , vol.65 , Issue.2 , pp. 122-132
    • Wasilko, D.J.1
  • 48
    • 84884191859 scopus 로고    scopus 로고
    • Tandem recombineering by SLIC cloning and Cre-LoxP fusion to generate multigene expression constructs for protein complex research
    • Haffke M, Viola C, Nie Y, Berger I (2013) Tandem recombineering by SLIC cloning and Cre-LoxP fusion to generate multigene expression constructs for protein complex research. Methods Mol Biol 1073:131–140
    • (2013) Methods Mol Biol , vol.1073 , pp. 131-140
    • Haffke, M.1    Viola, C.2    Nie, Y.3    Berger, I.4
  • 49
    • 0141618506 scopus 로고    scopus 로고
    • Spontaneous excision of BAC vector sequences from bacmid-derived baculovirus expression vectors upon passage in insect cells
    • Plijman GP, van Schijndel JE, Vlak JM (2003) Spontaneous excision of BAC vector sequences from bacmid-derived baculovirus expression vectors upon passage in insect cells. J Gen Virol 84:2669–2678
    • (2003) J Gen Virol , vol.84 , pp. 2669-2678
    • Plijman, G.P.1    Van Schijndel, J.E.2    Vlak, J.M.3
  • 50
    • 84879167660 scopus 로고    scopus 로고
    • Gene gymnastics: Synthetic biology for baculovirus expression vector system engineering
    • Vijachandran LS et al (2013) Gene gymnastics: synthetic biology for baculovirus expression vector system engineering. Bioengineered 4(5):279–287
    • (2013) Bioengineered , vol.4 , Issue.5 , pp. 279-287
    • Vijachandran, L.S.1
  • 53
    • 84879145033 scopus 로고    scopus 로고
    • Baculovirus expression: Tackling the complexity challenge
    • Barford D, Takagi Y, Schultz P, Berger I (2013) Baculovirus expression: tackling the complexity challenge. Curr Opin Struct Biol 23(3):357–364
    • (2013) Curr Opin Struct Biol , vol.23 , Issue.3 , pp. 357-364
    • Barford, D.1    Takagi, Y.2    Schultz, P.3    Berger, I.4
  • 54
    • 84923073621 scopus 로고    scopus 로고
    • Cytoplasmic TAF2-TAF8- TAF10 complex provides evidence for nuclear holo- TFIID assembly from preformed submodules
    • Trowitzsch S et al (2015) Cytoplasmic TAF2-TAF8- TAF10 complex provides evidence for nuclear holo- TFIID assembly from preformed submodules. Nat Commun 6:6011
    • (2015) Nat Commun , vol.6 , pp. 6011
    • Trowitzsch, S.1
  • 57
    • 84879148499 scopus 로고    scopus 로고
    • Protein production for structural biology: New solutions to new challenges
    • Berger I, Mary LM (2013) Protein production for structural biology: new solutions to new challenges. Curr Opin Struct Biol 23(3):317–318
    • (2013) Curr Opin Struct Biol , vol.23 , Issue.3 , pp. 317-318
    • Berger, I.1    Mary, L.M.2
  • 58
    • 84892545792 scopus 로고    scopus 로고
    • More pieces to the puzzle: Recent structural insights into class II transcription initiation
    • Kandiah E, Trowitzsch S, Gupta K, Haffke M, Berger I (2014) More pieces to the puzzle: recent structural insights into class II transcription initiation. Curr Opin Struct Biol 24:91–97
    • (2014) Curr Opin Struct Biol , vol.24 , pp. 91-97
    • Kandiah, E.1    Trowitzsch, S.2    Gupta, K.3    Haffke, M.4    Berger, I.5
  • 60
    • 79955547248 scopus 로고    scopus 로고
    • Structure and mechanism of the chromatin remodelling factor ISW1a
    • Yamada K et al (2011) Structure and mechanism of the chromatin remodelling factor ISW1a. Nature 472(7344):448–453
    • (2011) Nature , vol.472 , Issue.7344 , pp. 448-453
    • Yamada, K.1
  • 63
    • 84867913431 scopus 로고    scopus 로고
    • Structural basis for functional cooperation between tandem helicase cassettes in Brr2-mediated remodeling of the spliceosome
    • USA
    • Santos KF et al (2012) Structural basis for functional cooperation between tandem helicase cassettes in Brr2-mediated remodeling of the spliceosome. Proc Natl Acad Sci USA 109(43):17418–17423
    • (2012) Proc Natl Acad Sci , vol.109 , Issue.43 , pp. 17418-17423
    • Santos, K.F.1
  • 69
    • 84923319299 scopus 로고    scopus 로고
    • Reconstitution of active human core mediator complex reveals a critical role of the MED14 subunit
    • Cevher MA et al (2014) Reconstitution of active human core mediator complex reveals a critical role of the MED14 subunit. Nat Struct Mol Biol 21(12):1028–1034
    • (2014) Nat Struct Mol Biol , vol.21 , Issue.12 , pp. 1028-1034
    • Cevher, M.A.1
  • 70
    • 84908199292 scopus 로고    scopus 로고
    • Screening and large-scale expression of membrane proteins in mammalian cells for structural studies
    • Goehring A et al (2014) Screening and large-scale expression of membrane proteins in mammalian cells for structural studies. Nat Protoc 9(11):2574–2585
    • (2014) Nat Protoc , vol.9 , Issue.11 , pp. 2574-2585
    • Goehring, A.1
  • 71
    • 84864946465 scopus 로고    scopus 로고
    • Insect cells as factories for biomanufacturing
    • Drugmand JC, Schneider YJ, Agathos SN (2012) Insect cells as factories for biomanufacturing. Biotechnol Adv 30(5):1140–1157
    • (2012) Biotechnol Adv , vol.30 , Issue.5 , pp. 1140-1157
    • Drugmand, J.C.1    Schneider, Y.J.2    Agathos, S.N.3
  • 73
    • 77954833892 scopus 로고    scopus 로고
    • Improved expression of secreted and membrane-targeted proteins in insect cells
    • Hitchman RB et al (2010) Improved expression of secreted and membrane-targeted proteins in insect cells. Biotechnol Appl Biochem 56:85–93
    • (2010) Biotechnol Appl Biochem , vol.56 , pp. 85-93
    • Hitchman, R.B.1
  • 74
    • 5644293139 scopus 로고    scopus 로고
    • Development of a chitinase and v-cathepsin negative bacmid of improved integrity of secreted recombinant proteins
    • Kaba SA, Salceda AM, Wafula PO, Vlak JM, van Oers MM (2004) Development of a chitinase and v-cathepsin negative bacmid of improved integrity of secreted recombinant proteins. J Virol Methods 122:113–118
    • (2004) J Virol Methods , vol.122 , pp. 113-118
    • Kaba, S.A.1    Salceda, A.M.2    Wafula, P.O.3    Vlak, J.M.4    Van Oers, M.M.5
  • 75
    • 33748742271 scopus 로고    scopus 로고
    • Protein N-glycosylation in the baculovirus-insect cell system and engineering of insect cells to produce “mammalianized” recombinant glycoproteins
    • Harrison RL, Jarvis DL (2006) Protein N-glycosylation in the baculovirus-insect cell system and engineering of insect cells to produce “mammalianized” recombinant glycoproteins. Adv Virus Res 68:159–191
    • (2006) Adv Virus Res , vol.68 , pp. 159-191
    • Harrison, R.L.1    Jarvis, D.L.2
  • 76
    • 36048982078 scopus 로고    scopus 로고
    • Transforming lepidopteran insect cells for improved protein processing
    • Harrison RL, Jarvis DL (2007) Transforming lepidopteran insect cells for improved protein processing. Methods Mol Biol 388:341–356
    • (2007) Methods Mol Biol , vol.388 , pp. 341-356
    • Harrison, R.L.1    Jarvis, D.L.2
  • 78
    • 84876006230 scopus 로고    scopus 로고
    • Effective chickungunya viruslike particle vaccine produced in insect cells
    • Metz SW et al (2013) Effective chickungunya viruslike particle vaccine produced in insect cells. PLoS Negl Trop Dis 7:e2124
    • (2013) Plos Negl Trop Dis , vol.7
    • Metz, S.W.1
  • 80
    • 79960631586 scopus 로고    scopus 로고
    • Arbovirus vaccines: Opportunities for the baculovirus-insect cell expression system
    • Metz SW, Plijman GP (2011) Arbovirus vaccines: opportunities for the baculovirus-insect cell expression system. J Invertebr Pathol 107(Suppl):S16–S30
    • (2011) J Invertebr Pathol , vol.107
    • Metz, S.W.1    Plijman, G.P.2
  • 81
    • 84889690123 scopus 로고    scopus 로고
    • Baculoviral co-expression of HA, NA and M1 proteins of highly pathogenic H5N1 influenza virus in insect cells
    • Behzadian F et al (2013) Baculoviral co-expression of HA, NA and M1 proteins of highly pathogenic H5N1 influenza virus in insect cells. Jundishapur J Microbiol 6(9):e7665
    • (2013) Jundishapur J Microbiol , vol.6 , Issue.9
    • Behzadian, F.1
  • 82
    • 35348888341 scopus 로고    scopus 로고
    • Baculovirus expression vectors for insect and mammalian cells
    • Condreay JP, Kost TA (2007) Baculovirus expression vectors for insect and mammalian cells. Curr Drug Targets 8(10):1126–1131
    • (2007) Curr Drug Targets , vol.8 , Issue.10 , pp. 1126-1131
    • Condreay, J.P.1    Kost, T.A.2
  • 83
    • 37349084541 scopus 로고    scopus 로고
    • BacMam technology and its application to drug discovery
    • Ames RS, Kost TA, Condreay JP (2007) BacMam technology and its application to drug discovery. Expert Opin Drug Discov 2(12):1669–1681
    • (2007) Expert Opin Drug Discov , vol.2 , Issue.12 , pp. 1669-1681
    • Ames, R.S.1    Kost, T.A.2    Condreay, J.P.3
  • 84
    • 77953661678 scopus 로고    scopus 로고
    • Baculovirus gene delivery: A flexible assay development tool
    • Kost TA, Condreay JP, Ames RS (2010) Baculovirus gene delivery: a flexible assay development tool. Curr Gene Ther 10(3):168–173
    • (2010) Curr Gene Ther , vol.10 , Issue.3 , pp. 168-173
    • Kost, T.A.1    Condreay, J.P.2    Ames, R.S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.