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Volumn 73, Issue 2, 2010, Pages 209-216

Efficient production of human Fas receptor extracellular domain-human IgG1 heavy chain Fc domain fusion protein using baculovirus/silkworm expression system

Author keywords

Baculovirus; Fas ligand; Fas receptor; Fc domain; Secretory expression; Silkworm

Indexed keywords

FAS LIGAND; HYBRID PROTEIN; IMMUNOGLOBULIN FC FRAGMENT; IMMUNOGLOBULIN G; IMMUNOGLOBULIN HEAVY CHAIN; IMMUNOLOGIC FACTOR;

EID: 77955418167     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pep.2010.05.007     Document Type: Article
Times cited : (9)

References (36)
  • 4
    • 0030892234 scopus 로고    scopus 로고
    • Apoptosis by death factor
    • S. Nagata Apoptosis by death factor Cell 88 1997 355 365
    • (1997) Cell , vol.88 , pp. 355-365
    • Nagata, S.1
  • 5
    • 0037273852 scopus 로고    scopus 로고
    • Protein-based therapeutic approaches targeting death receptors
    • L.E. French, and J. Tschopp Protein-based therapeutic approaches targeting death receptors Cell Death Differ. 10 2003 117 123
    • (2003) Cell Death Differ. , vol.10 , pp. 117-123
    • French, L.E.1    Tschopp, J.2
  • 6
    • 0031002790 scopus 로고    scopus 로고
    • Essential roles of the Fas ligand in the development of hepatitis
    • T. Kondo, T. Suda, H. Fukuyama, M. Adachi, and S. Nagata Essential roles of the Fas ligand in the development of hepatitis Nat. Med. 3 1997 409 413
    • (1997) Nat. Med. , vol.3 , pp. 409-413
    • Kondo, T.1    Suda, T.2    Fukuyama, H.3    Adachi, M.4    Nagata, S.5
  • 8
    • 33646374671 scopus 로고    scopus 로고
    • Suppression of the cell-mediated immune response by a Fas-immunoglobulin fusion protein
    • Y. Shen, B. Young, and M.L. Lipman Suppression of the cell-mediated immune response by a Fas-immunoglobulin fusion protein Transplantation 81 2006 1041 1048
    • (2006) Transplantation , vol.81 , pp. 1041-1048
    • Shen, Y.1    Young, B.2    Lipman, M.L.3
  • 9
    • 77955413943 scopus 로고    scopus 로고
    • cited05.24.10
    • , 2010 (cited 05.24.10).
    • (2010)
  • 11
    • 41549097673 scopus 로고    scopus 로고
    • Cloning and purification of functionally active Fas ligand interfering protein (FIP) expressed in Escherichia coli
    • P. Wisniewski, A. Master, and B. Kaminska Cloning and purification of functionally active Fas ligand interfering protein (FIP) expressed in Escherichia coli Acta Biochim. Pol. 55 2008 51 56
    • (2008) Acta Biochim. Pol. , vol.55 , pp. 51-56
    • Wisniewski, P.1    Master, A.2    Kaminska, B.3
  • 12
    • 70449706366 scopus 로고    scopus 로고
    • Receptor-Fc fusion therapeutics, traps, and MIMETIBODY™ technology
    • C. Huang Receptor-Fc fusion therapeutics, traps, and MIMETIBODY™ technology Curr. Opin. Biotechnol. 20 2009 692 699
    • (2009) Curr. Opin. Biotechnol. , vol.20 , pp. 692-699
    • Huang, C.1
  • 13
    • 0032032327 scopus 로고    scopus 로고
    • Soluble FasR ligand-binding domain: High-yield production of active fusion and non-fusion recombinant proteins using the baculovirus/insect cell system
    • J. Mahiou, J.-P. Abastado, L. Cabinie, and F. Godeau Soluble FasR ligand-binding domain: high-yield production of active fusion and non-fusion recombinant proteins using the baculovirus/insect cell system Biochem. J. 330 1998 1051 1058
    • (1998) Biochem. J. , vol.330 , pp. 1051-1058
    • Mahiou, J.1    Abastado, J.-P.2    Cabinie, L.3    Godeau, F.4
  • 14
    • 0033927804 scopus 로고    scopus 로고
    • Expression of lymphotoxins and their receptor-Fc fusion proteins by baculovirus
    • I. Rooney, K. Butrovich, and C.F. Ware Expression of lymphotoxins and their receptor-Fc fusion proteins by baculovirus Methods Enzymol. 322 2000 345 363
    • (2000) Methods Enzymol. , vol.322 , pp. 345-363
    • Rooney, I.1    Butrovich, K.2    Ware, C.F.3
  • 16
    • 34547098850 scopus 로고    scopus 로고
    • Requirement of N-glycosylation for the secretion of recombinant extracellular domain of human Fas in HeLa cells
    • Y. Li, X. Yang, A.H.T. Nguyen, and I. Brockhausen Requirement of N-glycosylation for the secretion of recombinant extracellular domain of human Fas in HeLa cells Int. J. Biochem. Cell Biol. 39 2007 1625 1636
    • (2007) Int. J. Biochem. Cell Biol. , vol.39 , pp. 1625-1636
    • Li, Y.1    Yang, X.2    Nguyen, A.H.T.3    Brockhausen, I.4
  • 17
    • 33750813509 scopus 로고    scopus 로고
    • Secretory expression of synthetic human Fas ligand extracellular domain gene in Pichia pastoris: Influences of tag addition and N-glycosylation site deletion, and development of a purification method
    • M. Muraki Secretory expression of synthetic human Fas ligand extracellular domain gene in Pichia pastoris: influences of tag addition and N-glycosylation site deletion, and development of a purification method Protein Expr. Purif. 50 2006 137 146
    • (2006) Protein Expr. Purif. , vol.50 , pp. 137-146
    • Muraki, M.1
  • 18
    • 45449106344 scopus 로고    scopus 로고
    • Improved secretion of human Fas ligand extracellular domain by N-terminal part truncation in Pichia pastoris and preparation of the N-linked carbohydrate chain trimmed derivative
    • M. Muraki Improved secretion of human Fas ligand extracellular domain by N-terminal part truncation in Pichia pastoris and preparation of the N-linked carbohydrate chain trimmed derivative Protein Expr. Purif. 60 2008 205 213
    • (2008) Protein Expr. Purif. , vol.60 , pp. 205-213
    • Muraki, M.1
  • 19
    • 0035166478 scopus 로고    scopus 로고
    • Baculovirus expression cassette vectors for rapid production of complete human IgG from phage display selected antibody fragments
    • M. Liang, S. Dübel, D. Li, I. Queitsch, W. Li, and E.K.F. Bautz Baculovirus expression cassette vectors for rapid production of complete human IgG from phage display selected antibody fragments J. Immunol. Methods 247 2001 119 130
    • (2001) J. Immunol. Methods , vol.247 , pp. 119-130
    • Liang, M.1    Dübel, S.2    Li, D.3    Queitsch, I.4    Li, W.5    Bautz, E.K.F.6
  • 20
    • 77955414989 scopus 로고    scopus 로고
    • cited18.03.10
    • < http://www.kazusa.or.jp/codon/cgi-bin/showcodon.cgi?species=46015 >, 2010 (cited 18.03.10).
    • (2010)
  • 21
    • 0026084931 scopus 로고
    • Structures and organization of major plasma protein genes of the silkworm Bombyx mori
    • S. Mori, S. Izumi, and S. Tomino Structures and organization of major plasma protein genes of the silkworm Bombyx mori J. Mol. Biol. 218 1991 7 12
    • (1991) J. Mol. Biol. , vol.218 , pp. 7-12
    • Mori, S.1    Izumi, S.2    Tomino, S.3
  • 22
    • 75549087467 scopus 로고    scopus 로고
    • Recombinant protein production by a kaiko-baculovirus system
    • H. Nagaya Recombinant protein production by a kaiko-baculovirus system H. Koga, Methods in Molecular Biology, Reverse Chemical Genetics vol. 577 2009 Humana Press Inc. 109 120
    • (2009) Methods in Molecular Biology, Reverse Chemical Genetics , vol.577 , pp. 109-120
    • Nagaya, H.1
  • 24
    • 71549161144 scopus 로고    scopus 로고
    • Physical instability of a therapeutic Fc fusion protein: Domain contributions to conformational and colloidal stability
    • J.L. Fast, A.A. Cordes, J.F. Carpenter, and T.W. Randolph Physical instability of a therapeutic Fc fusion protein: domain contributions to conformational and colloidal stability Biochemistry 48 2009 11724 11736
    • (2009) Biochemistry , vol.48 , pp. 11724-11736
    • Fast, J.L.1    Cordes, A.A.2    Carpenter, J.F.3    Randolph, T.W.4
  • 25
    • 0001090047 scopus 로고
    • Molecular properties and biosynthesis of major plasma proteins in Bombyx mori
    • S. Izumi, J. Fujie, S. Yamada, and S. Tomino Molecular properties and biosynthesis of major plasma proteins in Bombyx mori Biochim. Biophys. Acta 670 1981 222 229
    • (1981) Biochim. Biophys. Acta , vol.670 , pp. 222-229
    • Izumi, S.1    Fujie, J.2    Yamada, S.3    Tomino, S.4
  • 26
    • 0023881356 scopus 로고
    • Trends in the development of baculovirus expression vectors
    • V.A. Lucknow, and M.D. Summers Trends in the development of baculovirus expression vectors Biotechnology 6 1988 47 55
    • (1988) Biotechnology , vol.6 , pp. 47-55
    • Lucknow, V.A.1    Summers, M.D.2
  • 29
    • 43449088501 scopus 로고    scopus 로고
    • Expression of the extracellular region of the human interleukin-4 receptor α chain and interleukin-13 receptor α1 chain by a silkworm-baculovirus system
    • E. Honjo, Y. Shoyama, T. Tamada, H. Shigematsu, T. Hatanaka, S. Kanaji, K. Arima, Y. Ito, K. Izuhara, and R. Kuroki Expression of the extracellular region of the human interleukin-4 receptor α chain and interleukin-13 receptor α1 chain by a silkworm-baculovirus system Protein Expr. Purif. 60 2008 25 30
    • (2008) Protein Expr. Purif. , vol.60 , pp. 25-30
    • Honjo, E.1    Shoyama, Y.2    Tamada, T.3    Shigematsu, H.4    Hatanaka, T.5    Kanaji, S.6    Arima, K.7    Ito, Y.8    Izuhara, K.9    Kuroki, R.10
  • 31
    • 70349386086 scopus 로고    scopus 로고
    • Establishment of human lysozyme mass production system using insect factory, silkworm larvae
    • Y. Tsuchiya, J. Shirai, and S. Inumaru Establishment of human lysozyme mass production system using insect factory, silkworm larvae Jpn. Agric. Res. Q. 43 2009 207 212
    • (2009) Jpn. Agric. Res. Q. , vol.43 , pp. 207-212
    • Tsuchiya, Y.1    Shirai, J.2    Inumaru, S.3
  • 32
    • 0346096508 scopus 로고    scopus 로고
    • Quality control in the endoplasmic reticulum protein factory
    • R. Sitia, and I. Braakman Quality control in the endoplasmic reticulum protein factory Nature 426 2003 891 894
    • (2003) Nature , vol.426 , pp. 891-894
    • Sitia, R.1    Braakman, I.2
  • 33
    • 0028774540 scopus 로고
    • Expression of highly disulfide-bonded proteins in Pichia pastoris
    • C.E. White, N.M. Kempi, and E.A. Komives Expression of highly disulfide-bonded proteins in Pichia pastoris Structure 2 1994 1003 1005
    • (1994) Structure , vol.2 , pp. 1003-1005
    • White, C.E.1    Kempi, N.M.2    Komives, E.A.3
  • 34
    • 0033955337 scopus 로고    scopus 로고
    • Heterologous protein expression in the methylotrophic yeast Pichia pastoris
    • J.L. Cereghino, and J.M. Cregg Heterologous protein expression in the methylotrophic yeast Pichia pastoris FEMS Microbiol. Rev. 24 2000 45 66
    • (2000) FEMS Microbiol. Rev. , vol.24 , pp. 45-66
    • Cereghino, J.L.1    Cregg, J.M.2
  • 36
    • 0030684009 scopus 로고    scopus 로고
    • Requirement of cysteine-rich repeats of the Fas receptor for binding by the Fas ligand
    • J.R. Orlinick, A. Vaishnaw, K.B. Elkon, and M.V. Chao Requirement of cysteine-rich repeats of the Fas receptor for binding by the Fas ligand J. Biol. Chem. 272 1997 28889 28894
    • (1997) J. Biol. Chem. , vol.272 , pp. 28889-28894
    • Orlinick, J.R.1    Vaishnaw, A.2    Elkon, K.B.3    Chao, M.V.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.