메뉴 건너뛰기




Volumn 63, Issue 6, 2008, Pages 1401-1414

Preparing recombinant single chain antibodies

Author keywords

Biomolecular engineering; Biomolecule; Processing; Protein; Recombinant antibodies; Single chain variable fragment

Indexed keywords

ANTIGENS; BIOMOLECULES; CONSTRAINT THEORY; IMMUNOLOGY;

EID: 38949210239     PISSN: 00092509     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ces.2007.11.022     Document Type: Review
Times cited : (24)

References (139)
  • 1
    • 33845971450 scopus 로고    scopus 로고
    • Novel single chain antibodies to the prion protein identified by phage display
    • Adamson C.S., Yao Y., Vasiljevic S., Sy M.S., Ren J., and Jones I.M. Novel single chain antibodies to the prion protein identified by phage display. Virology 358 (2007) 166-177
    • (2007) Virology , vol.358 , pp. 166-177
    • Adamson, C.S.1    Yao, Y.2    Vasiljevic, S.3    Sy, M.S.4    Ren, J.5    Jones, I.M.6
  • 3
    • 0345195967 scopus 로고    scopus 로고
    • Factors influencing the dimer to monomer transition of an antibody single-chain Fv fragment
    • Arndt K.M., Muller K.M., and Pluckthun A. Factors influencing the dimer to monomer transition of an antibody single-chain Fv fragment. Biochemistry 37 (1998) 12918-12926
    • (1998) Biochemistry , vol.37 , pp. 12918-12926
    • Arndt, K.M.1    Muller, K.M.2    Pluckthun, A.3
  • 4
    • 0035197422 scopus 로고    scopus 로고
    • Recombinant scFv/streptavidin-binding peptide fusion protein for the quantitative determination of the scorpion venom neurotoxin Aahl
    • Aubrey N., Devaux C., di Luccio E., Goyffon M., Rochat H., and Billiald P. Recombinant scFv/streptavidin-binding peptide fusion protein for the quantitative determination of the scorpion venom neurotoxin Aahl. Biological Chemistry 382 (2001) 1621-1628
    • (2001) Biological Chemistry , vol.382 , pp. 1621-1628
    • Aubrey, N.1    Devaux, C.2    di Luccio, E.3    Goyffon, M.4    Rochat, H.5    Billiald, P.6
  • 5
    • 0035823143 scopus 로고    scopus 로고
    • Escherichia coli maltose-binding protein as a molecular chaperone for recombinant intracellular cytoplasmic single-chain antibodies
    • Bach H., Mazor Y., Shaky S., Shoham-Lev A., Berdichevsky Y., Gutnick D.L., and Benhar I. Escherichia coli maltose-binding protein as a molecular chaperone for recombinant intracellular cytoplasmic single-chain antibodies. Journal of Molecular Biology 312 (2001) 79-93
    • (2001) Journal of Molecular Biology , vol.312 , pp. 79-93
    • Bach, H.1    Mazor, Y.2    Shaky, S.3    Shoham-Lev, A.4    Berdichevsky, Y.5    Gutnick, D.L.6    Benhar, I.7
  • 6
    • 28144460981 scopus 로고    scopus 로고
    • Inteins and affinity resin substitutes for protein purification and scale up
    • Banki M.R., and Wood D.W. Inteins and affinity resin substitutes for protein purification and scale up. Microbial Cell Factories 4:32 (2005) 1-6
    • (2005) Microbial Cell Factories , vol.4 32 , pp. 1-6
    • Banki, M.R.1    Wood, D.W.2
  • 11
    • 0023922661 scopus 로고
    • Escherichia coli secretion of an active chimeric antibody fragment
    • Better M., Chang C.P., Robinson R.R., and Horwitz A.H. Escherichia coli secretion of an active chimeric antibody fragment. Science 242 (1988) 1041-1043
    • (1988) Science , vol.242 , pp. 1041-1043
    • Better, M.1    Chang, C.P.2    Robinson, R.R.3    Horwitz, A.H.4
  • 13
    • 0036517707 scopus 로고    scopus 로고
    • Self-immobilising recombinant antibody fragments for immunoaffinity chromatography: generic, parallel, and scalable protein purification
    • Blank K., Lindner P., Diefenback B., and Pluckthun A. Self-immobilising recombinant antibody fragments for immunoaffinity chromatography: generic, parallel, and scalable protein purification. Protein Expression and Purification 24 (2002) 313-322
    • (2002) Protein Expression and Purification , vol.24 , pp. 313-322
    • Blank, K.1    Lindner, P.2    Diefenback, B.3    Pluckthun, A.4
  • 15
    • 0028011935 scopus 로고
    • Bifunctional hybrids between the variable domains of an immunoglobulin and the maltose-binding protein of Escherichia coli-production, purification and antigen-binding
    • Bregegere F., Schwartz J., and Bedoulle H. Bifunctional hybrids between the variable domains of an immunoglobulin and the maltose-binding protein of Escherichia coli-production, purification and antigen-binding. Protein Engineering 7 (1994) 271-280
    • (1994) Protein Engineering , vol.7 , pp. 271-280
    • Bregegere, F.1    Schwartz, J.2    Bedoulle, H.3
  • 16
    • 33645509276 scopus 로고    scopus 로고
    • CD7-restricted activation of Fas-mediated apoptosis: a novel therapeutic approach for acute T-cell leukaemia
    • Bremer E., ten Cate B., Samplonius D.F., de Leij L.F.M., and Helfrich W. CD7-restricted activation of Fas-mediated apoptosis: a novel therapeutic approach for acute T-cell leukaemia. Immunobiology 107 (2006) 2863-2870
    • (2006) Immunobiology , vol.107 , pp. 2863-2870
    • Bremer, E.1    ten Cate, B.2    Samplonius, D.F.3    de Leij, L.F.M.4    Helfrich, W.5
  • 17
    • 32944464376 scopus 로고    scopus 로고
    • Production and characterization of a bacterial single-chain antibody fragment specific to B-cell-activating factor of the TNF family
    • Cao P., Tang X.M., Guan Z.B., Diao Z.Y., and Zhang S.Q. Production and characterization of a bacterial single-chain antibody fragment specific to B-cell-activating factor of the TNF family. Protein Expression and Purification 43 (2005) 157-164
    • (2005) Protein Expression and Purification , vol.43 , pp. 157-164
    • Cao, P.1    Tang, X.M.2    Guan, Z.B.3    Diao, Z.Y.4    Zhang, S.Q.5
  • 19
    • 0030949407 scopus 로고    scopus 로고
    • Production of a soluble and active MBP-scFv fusion: favourable effect of the leaky tolR strain
    • Chames P., Fieschi J., and Batty D. Production of a soluble and active MBP-scFv fusion: favourable effect of the leaky tolR strain. FEBS Letters 405 (1997) 224-228
    • (1997) FEBS Letters , vol.405 , pp. 224-228
    • Chames, P.1    Fieschi, J.2    Batty, D.3
  • 20
    • 0037124466 scopus 로고    scopus 로고
    • PEGylated antibodies and antibody fragments for improved therapy: a review
    • Chapman A.P. PEGylated antibodies and antibody fragments for improved therapy: a review. Advanced Drug Delivery Reviews 54 (2002) 531-545
    • (2002) Advanced Drug Delivery Reviews , vol.54 , pp. 531-545
    • Chapman, A.P.1
  • 22
    • 33746831621 scopus 로고    scopus 로고
    • Construction of three single-chain antibody fragment variable fusion structures for sensitive detection of nucleocapsid protein of Hantaan virus
    • Chen J., Xie W.H., Zhang Z.P., Zhang X.E., Li W., Wang S.H., Zhou Y.F., Liang M.F., Wang K.M., and Yang Z.Q. Construction of three single-chain antibody fragment variable fusion structures for sensitive detection of nucleocapsid protein of Hantaan virus. Analytical Letters 39 (2006) 2153-2167
    • (2006) Analytical Letters , vol.39 , pp. 2153-2167
    • Chen, J.1    Xie, W.H.2    Zhang, Z.P.3    Zhang, X.E.4    Li, W.5    Wang, S.H.6    Zhou, Y.F.7    Liang, M.F.8    Wang, K.M.9    Yang, Z.Q.10
  • 23
    • 0032511990 scopus 로고    scopus 로고
    • Characterization of a new intrabody directed against the N-terminal region of human p53
    • Cohen P.A., Mani J.C., and Lane D.P. Characterization of a new intrabody directed against the N-terminal region of human p53. Oncogene 17 (1998) 2445-2456
    • (1998) Oncogene , vol.17 , pp. 2445-2456
    • Cohen, P.A.1    Mani, J.C.2    Lane, D.P.3
  • 24
    • 14744299579 scopus 로고
    • Recent advances in the expression of foreign genes in Pichia pastoris
    • Cregg J.M., Vedvick T.S., and Raschke W.C. Recent advances in the expression of foreign genes in Pichia pastoris. BioTechnology 11 (1993) 905-910
    • (1993) BioTechnology , vol.11 , pp. 905-910
    • Cregg, J.M.1    Vedvick, T.S.2    Raschke, W.C.3
  • 29
    • 0032146168 scopus 로고    scopus 로고
    • In vivo retargeting of T cell effector function by recombinant bispecific single chain Fv (anti-CD 3 × anti-idiotype), induces long-term survival in the murine BCL1 lymphoma model
    • De Jonge J., Heirman C., de Veerman M., Van Meirvenne S., Moser M., Leo O., and Thielemans K. In vivo retargeting of T cell effector function by recombinant bispecific single chain Fv (anti-CD 3 × anti-idiotype), induces long-term survival in the murine BCL1 lymphoma model. Journal of Immunology 161 (1998) 1454-1461
    • (1998) Journal of Immunology , vol.161 , pp. 1454-1461
    • De Jonge, J.1    Heirman, C.2    de Veerman, M.3    Van Meirvenne, S.4    Moser, M.5    Leo, O.6    Thielemans, K.7
  • 31
    • 0028068099 scopus 로고
    • Mammalian cell expression of single-chain Fv (sFv) antibody proteins and their C-terminal fusions with interleukin-2 and other effector domains
    • Dorai H., McCartney J.E., Hudziak R.M., Tai M.S., Laminet A.A., Houston L.L., Huston J.S., and Oppermann H. Mammalian cell expression of single-chain Fv (sFv) antibody proteins and their C-terminal fusions with interleukin-2 and other effector domains. BioTechnology 12 (1994) 890-897
    • (1994) BioTechnology , vol.12 , pp. 890-897
    • Dorai, H.1    McCartney, J.E.2    Hudziak, R.M.3    Tai, M.S.4    Laminet, A.A.5    Houston, L.L.6    Huston, J.S.7    Oppermann, H.8
  • 33
    • 0027975979 scopus 로고
    • Intra- and extracellular expression of an scFv antibody fragment in E. coli: effect of bacterial strains and pathway engineering using GroES/L chaperonins.
    • Duenas M., Vazquez J., Ayala M., Soderlind E., Ohlin M., Perez L., Borrebaeck C.A., and Gavilondo J.V. Intra- and extracellular expression of an scFv antibody fragment in E. coli: effect of bacterial strains and pathway engineering using GroES/L chaperonins. BioTechniques 16 (1994) 476-482
    • (1994) BioTechniques , vol.16 , pp. 476-482
    • Duenas, M.1    Vazquez, J.2    Ayala, M.3    Soderlind, E.4    Ohlin, M.5    Perez, L.6    Borrebaeck, C.A.7    Gavilondo, J.V.8
  • 35
    • 0027471898 scopus 로고
    • Specific activation and targeting of cytotoxic lymphocytes through chimeric single chains consisting of antibody-binding domains and the γ or ζ subunits of the immunoglobulin and T-cell receptors
    • Eshhar Z., Waks T., Gross G., and Schindler D.G. Specific activation and targeting of cytotoxic lymphocytes through chimeric single chains consisting of antibody-binding domains and the γ or ζ subunits of the immunoglobulin and T-cell receptors. Proceedings of the National Academy of Sciences of the United States of America 90 (1993) 720-724
    • (1993) Proceedings of the National Academy of Sciences of the United States of America , vol.90 , pp. 720-724
    • Eshhar, Z.1    Waks, T.2    Gross, G.3    Schindler, D.G.4
  • 36
    • 3142682191 scopus 로고    scopus 로고
    • Yeast display of antibody fragments: a discovery and characterization platform
    • Feldhaus M.J., and Siegel R.W. Yeast display of antibody fragments: a discovery and characterization platform. Journal of Immunological Methods 290 (2004) 69-80
    • (2004) Journal of Immunological Methods , vol.290 , pp. 69-80
    • Feldhaus, M.J.1    Siegel, R.W.2
  • 37
    • 0028889621 scopus 로고
    • High-level production and long-term storage of engineered antibodies in transgenic tobacco seeds
    • Fiedler U., and Conrad U. High-level production and long-term storage of engineered antibodies in transgenic tobacco seeds. BioTechnology 13 (1995) 1090-1093
    • (1995) BioTechnology , vol.13 , pp. 1090-1093
    • Fiedler, U.1    Conrad, U.2
  • 38
    • 34248551662 scopus 로고    scopus 로고
    • Antibody engineering and modification technologies
    • Fipula D. Antibody engineering and modification technologies. Biomolecular Engineering 24 (2007) 201-215
    • (2007) Biomolecular Engineering , vol.24 , pp. 201-215
    • Fipula, D.1
  • 39
    • 0032843939 scopus 로고    scopus 로고
    • Towards molecular farming in the future: Pichia pastoris-based production of single-chain antibody fragments
    • Fischer R., Drossard J., Emans N., Commandeur U., and Hellwig S. Towards molecular farming in the future: Pichia pastoris-based production of single-chain antibody fragments. Biotechnology and Applied Biochemistry 30 (1999) 117-120
    • (1999) Biotechnology and Applied Biochemistry , vol.30 , pp. 117-120
    • Fischer, R.1    Drossard, J.2    Emans, N.3    Commandeur, U.4    Hellwig, S.5
  • 41
    • 0027263307 scopus 로고
    • Antitumour activity of the single chain immunotoxin BR96 sFv-PE40 against established breast and lung tumour xenografts
    • Friedman P.N., Chace D.F., Trail P.A., and Siegall C.B. Antitumour activity of the single chain immunotoxin BR96 sFv-PE40 against established breast and lung tumour xenografts. Journal of Immunology 150 (1993) 3054-3061
    • (1993) Journal of Immunology , vol.150 , pp. 3054-3061
    • Friedman, P.N.1    Chace, D.F.2    Trail, P.A.3    Siegall, C.B.4
  • 43
    • 33846126638 scopus 로고    scopus 로고
    • Antibody production with yeasts and filamentous fungi: on the road to large scale?
    • Gasser B., and Mattanovich D. Antibody production with yeasts and filamentous fungi: on the road to large scale?. Biotechnology Letters 29 (2007) 201-212
    • (2007) Biotechnology Letters , vol.29 , pp. 201-212
    • Gasser, B.1    Mattanovich, D.2
  • 44
    • 0026572809 scopus 로고
    • The disulphide bonds in antibody variable domains: effects on stability, folding in vitro, and functional expression in E. coli
    • Glockshuber R., Schmidt T., and Pluckthun A. The disulphide bonds in antibody variable domains: effects on stability, folding in vitro, and functional expression in E. coli. Biochemistry 31 (1992) 1270-1279
    • (1992) Biochemistry , vol.31 , pp. 1270-1279
    • Glockshuber, R.1    Schmidt, T.2    Pluckthun, A.3
  • 45
    • 0034671309 scopus 로고    scopus 로고
    • Genetically engineered tetravalent single-chain Fv of the pancarcinoma monoclonal antibody CC49: improved biodistribution and potential for therapeutic application
    • Goel A., Colcher D., Baranowska-Kortylewicz J., Augustine S., Booth B.J.M., Pavlinkova G., and Batra S.K. Genetically engineered tetravalent single-chain Fv of the pancarcinoma monoclonal antibody CC49: improved biodistribution and potential for therapeutic application. Cancer Research 60 (2000) 6964-6971
    • (2000) Cancer Research , vol.60 , pp. 6964-6971
    • Goel, A.1    Colcher, D.2    Baranowska-Kortylewicz, J.3    Augustine, S.4    Booth, B.J.M.5    Pavlinkova, G.6    Batra, S.K.7
  • 46
    • 1042288100 scopus 로고    scopus 로고
    • High-level production in Pichia pastoris of an anti-p185(HER-2) single-chain antibody fragment using an alternative secretion expression vector
    • Gurkan C., Symeonides S.N., and Ellar D.J. High-level production in Pichia pastoris of an anti-p185(HER-2) single-chain antibody fragment using an alternative secretion expression vector. Biotechnology and Applied Biochemistry 39 (2004) 115-122
    • (2004) Biotechnology and Applied Biochemistry , vol.39 , pp. 115-122
    • Gurkan, C.1    Symeonides, S.N.2    Ellar, D.J.3
  • 47
    • 33646397008 scopus 로고    scopus 로고
    • Production of soluble and active transferrin receptor-targeting single-chain antibody using Saccharomyces cerevisiae
    • Hackel B.J., Huang D., Bubolz J.C., Wang X.X., and Shusta E.V. Production of soluble and active transferrin receptor-targeting single-chain antibody using Saccharomyces cerevisiae. Pharmaceutical Research 23 (2006) 790-797
    • (2006) Pharmaceutical Research , vol.23 , pp. 790-797
    • Hackel, B.J.1    Huang, D.2    Bubolz, J.C.3    Wang, X.X.4    Shusta, E.V.5
  • 48
    • 13244296815 scopus 로고    scopus 로고
    • Construction and characterization of a recombinant plasminogen activator composed of an anti-fibrin single chain antibody and low-molecular-weight urokinase
    • Hagemeyer C.E., Tomic I., Weirich U., Graeber J., Nordt T., Runge M.S., Bode C., and Peter K. Construction and characterization of a recombinant plasminogen activator composed of an anti-fibrin single chain antibody and low-molecular-weight urokinase. Journal of Thrombosis and Haemostasis 2 (2004) 797-803
    • (2004) Journal of Thrombosis and Haemostasis , vol.2 , pp. 797-803
    • Hagemeyer, C.E.1    Tomic, I.2    Weirich, U.3    Graeber, J.4    Nordt, T.5    Runge, M.S.6    Bode, C.7    Peter, K.8
  • 50
    • 0034142296 scopus 로고    scopus 로고
    • Improved expression characteristics of single-chain Fv fragments when fused downstream of the Escherichia coli maltose-binding protein or upstream of a single immunoglobulin-constant domain
    • Hayhurst A. Improved expression characteristics of single-chain Fv fragments when fused downstream of the Escherichia coli maltose-binding protein or upstream of a single immunoglobulin-constant domain. Protein Expression and Purification 18 (2000) 1-10
    • (2000) Protein Expression and Purification , vol.18 , pp. 1-10
    • Hayhurst, A.1
  • 51
    • 0038119665 scopus 로고    scopus 로고
    • Efficient inclusion body processing using chemical extraction and high gradient magnetic fishing
    • Heeboll-Nielsen A., Choe W.S., Middelberg A.P.J., and Thomas O.R.T. Efficient inclusion body processing using chemical extraction and high gradient magnetic fishing. Biotechnology Progress 19 (2003) 887-898
    • (2003) Biotechnology Progress , vol.19 , pp. 887-898
    • Heeboll-Nielsen, A.1    Choe, W.S.2    Middelberg, A.P.J.3    Thomas, O.R.T.4
  • 53
    • 27144432842 scopus 로고    scopus 로고
    • Engineered antibody fragments and the rise of single domains
    • Holliger P., and Hudson P.J. Engineered antibody fragments and the rise of single domains. Nature Biotechnology 23 (2005) 1126-1136
    • (2005) Nature Biotechnology , vol.23 , pp. 1126-1136
    • Holliger, P.1    Hudson, P.J.2
  • 54
    • 27144431943 scopus 로고    scopus 로고
    • Selecting and screening recombinant antibody libraries
    • Hoogenboom H.R. Selecting and screening recombinant antibody libraries. Nature Biotechnology 23 (2005) 1105-1116
    • (2005) Nature Biotechnology , vol.23 , pp. 1105-1116
    • Hoogenboom, H.R.1
  • 55
    • 16344379251 scopus 로고    scopus 로고
    • Secretion and surface display of green fluorescent protein using the yeast Saccharomyces cerevisiae
    • Huang D., and Shusta E.V. Secretion and surface display of green fluorescent protein using the yeast Saccharomyces cerevisiae. Biotechnology Progress 21 (2005) 349
    • (2005) Biotechnology Progress , vol.21 , pp. 349
    • Huang, D.1    Shusta, E.V.2
  • 56
    • 33845521492 scopus 로고    scopus 로고
    • A yeast platform for the production of single-chain antibody-green fluorescent protein fusions
    • Huang D., and Shusta E.V. A yeast platform for the production of single-chain antibody-green fluorescent protein fusions. Applied and Environmental Microbiology 72 (2006) 7748-7759
    • (2006) Applied and Environmental Microbiology , vol.72 , pp. 7748-7759
    • Huang, D.1    Shusta, E.V.2
  • 57
    • 0037026235 scopus 로고    scopus 로고
    • High-gradient magnetic affinity separation of trypsin from porcine pancreatin
    • Hubbuch J.J., and Thomas O.R.T. High-gradient magnetic affinity separation of trypsin from porcine pancreatin. Biotechnology and Bioengineering 79 (2002) 301-313
    • (2002) Biotechnology and Bioengineering , vol.79 , pp. 301-313
    • Hubbuch, J.J.1    Thomas, O.R.T.2
  • 58
    • 0032822839 scopus 로고    scopus 로고
    • Recombinant antibody constructs in cancer therapy
    • Hudson P.J. Recombinant antibody constructs in cancer therapy. Current Opinion in Immunology 11 (1999) 548-557
    • (1999) Current Opinion in Immunology , vol.11 , pp. 548-557
    • Hudson, P.J.1
  • 62
    • 33747649248 scopus 로고    scopus 로고
    • Oxygen-limited control of methanol uptake for improved production of a single-chain antibody fragment with recombinant Pichia pastoris
    • Khatri N.K., and Hoffmann F. Oxygen-limited control of methanol uptake for improved production of a single-chain antibody fragment with recombinant Pichia pastoris. Biotechnological Products and Process Engineering 72 (2006) 492-498
    • (2006) Biotechnological Products and Process Engineering , vol.72 , pp. 492-498
    • Khatri, N.K.1    Hoffmann, F.2
  • 63
    • 0942286940 scopus 로고    scopus 로고
    • Efficient production of a bioactive, multiple disulphide-bonded protein
    • Kim D.M., and Swartz J.R. Efficient production of a bioactive, multiple disulphide-bonded protein. Biotechnology and Bioengineering 85 (2004) 122-129
    • (2004) Biotechnology and Bioengineering , vol.85 , pp. 122-129
    • Kim, D.M.1    Swartz, J.R.2
  • 65
    • 0030916353 scopus 로고    scopus 로고
    • Two amino acid mutations in an anti-human CD3 single chain Fv antibody fragment that affect the yield on bacterial secretion but not the affinity
    • Kipriyanov S.M., Moldenhauer G., Martin A.C., Kupriyanova O.A., and Little M. Two amino acid mutations in an anti-human CD3 single chain Fv antibody fragment that affect the yield on bacterial secretion but not the affinity. Protein Engineering 10 (1997) 445-453
    • (1997) Protein Engineering , vol.10 , pp. 445-453
    • Kipriyanov, S.M.1    Moldenhauer, G.2    Martin, A.C.3    Kupriyanova, O.A.4    Little, M.5
  • 67
    • 0028966985 scopus 로고
    • Engineered turns of a recombinant antibody improve its in vivo folding
    • Knappik A., and Pluckthun A. Engineered turns of a recombinant antibody improve its in vivo folding. Protein Engineering 8 (1995) 81-89
    • (1995) Protein Engineering , vol.8 , pp. 81-89
    • Knappik, A.1    Pluckthun, A.2
  • 70
    • 0031973556 scopus 로고    scopus 로고
    • Expression and secretion of functional miniantibodies McPC603scFvDhlx in cell-wall-less L-form strains of Proteus mirabilis and Escherichia coli: a comparison of the synthesis capacities of L-form strains with an E. coli producer strain
    • Kujau M.J., Hoischen C., Riesenberg D., and Gumpert J. Expression and secretion of functional miniantibodies McPC603scFvDhlx in cell-wall-less L-form strains of Proteus mirabilis and Escherichia coli: a comparison of the synthesis capacities of L-form strains with an E. coli producer strain. Applied Microbiology and Biotechnology 49 (1998) 51-58
    • (1998) Applied Microbiology and Biotechnology , vol.49 , pp. 51-58
    • Kujau, M.J.1    Hoischen, C.2    Riesenberg, D.3    Gumpert, J.4
  • 71
    • 0025767916 scopus 로고
    • Strategies for improving plasmid stability in genetically modified bacteria in bioreactors
    • Kumar P.K.R., Maschke H.E., Friehs K., and Schugert K. Strategies for improving plasmid stability in genetically modified bacteria in bioreactors. Trends in Biotechnology 9 (1991) 279-284
    • (1991) Trends in Biotechnology , vol.9 , pp. 279-284
    • Kumar, P.K.R.1    Maschke, H.E.2    Friehs, K.3    Schugert, K.4
  • 74
    • 0036929881 scopus 로고    scopus 로고
    • Bacterial expression and in vitro refolding of a single-chain Fv antibody specific for human plasma apolipoprotein B-100
    • Lee M.H., Park T.I., Park Y.B., and Kwak J.W. Bacterial expression and in vitro refolding of a single-chain Fv antibody specific for human plasma apolipoprotein B-100. Protein Expression and Purification 25 (2002) 166-173
    • (2002) Protein Expression and Purification , vol.25 , pp. 166-173
    • Lee, M.H.1    Park, T.I.2    Park, Y.B.3    Kwak, J.W.4
  • 75
    • 3142685154 scopus 로고    scopus 로고
    • In-vitro protein evolution by ribosome display and mRNA display
    • Lipovsek D., and Pluckthun A. In-vitro protein evolution by ribosome display and mRNA display. Journal of Immunological Methods 290 (2004) 51-67
    • (2004) Journal of Immunological Methods , vol.290 , pp. 51-67
    • Lipovsek, D.1    Pluckthun, A.2
  • 76
    • 33645019759 scopus 로고    scopus 로고
    • Generation and characterization of a novel tetravalent anti-CD22 antibody with improved antitumor activity and pharmacokinetics
    • Liu X.Y., Pop L.M., Roopenian D.C., Ghetie V., Vitetta E.S., and Smallshaw J.E. Generation and characterization of a novel tetravalent anti-CD22 antibody with improved antitumor activity and pharmacokinetics. International Immunopharmacology 6 (2006) 791-799
    • (2006) International Immunopharmacology , vol.6 , pp. 791-799
    • Liu, X.Y.1    Pop, L.M.2    Roopenian, D.C.3    Ghetie, V.4    Vitetta, E.S.5    Smallshaw, J.E.6
  • 77
    • 27144492909 scopus 로고    scopus 로고
    • Transgenic tobacco plants expressing a dimeric single-chain variable fragment (scFv) antibody against Salmonella enterica serotype paratyphi B
    • Makvandi-Nejad S., McLean M.D., Hirama T., Almquist K.C., MacKenzie C.R., and Hall J.C. Transgenic tobacco plants expressing a dimeric single-chain variable fragment (scFv) antibody against Salmonella enterica serotype paratyphi B. Transgenic Research 14 (2005) 785-792
    • (2005) Transgenic Research , vol.14 , pp. 785-792
    • Makvandi-Nejad, S.1    McLean, M.D.2    Hirama, T.3    Almquist, K.C.4    MacKenzie, C.R.5    Hall, J.C.6
  • 78
    • 0026900383 scopus 로고
    • Expression of a Chlamydia anticarbohydrate single-chain antibody as a maltose binding fusion protein
    • Malinowski D.P., Gourley M., Edelstein S., and Pearson R.E. Expression of a Chlamydia anticarbohydrate single-chain antibody as a maltose binding fusion protein. Cell Biophysics 21 (1992) 1-12
    • (1992) Cell Biophysics , vol.21 , pp. 1-12
    • Malinowski, D.P.1    Gourley, M.2    Edelstein, S.3    Pearson, R.E.4
  • 79
    • 0032479180 scopus 로고    scopus 로고
    • Expression of an antibody fragment at high levels in the bacterial cytoplasm
    • Martineau P., Jones P., and Winter G. Expression of an antibody fragment at high levels in the bacterial cytoplasm. Journal of Molecular Biology 280 (1998) 117-127
    • (1998) Journal of Molecular Biology , vol.280 , pp. 117-127
    • Martineau, P.1    Jones, P.2    Winter, G.3
  • 80
    • 0026327378 scopus 로고
    • Construction, binding properties, metabolism, and tumor targeting of a single-chain Fv derived from the pancarcinoma monoclonal antibody CC49
    • Milenic D.E., Yokota T., Filpula D.R., Finkelman M.A.J., Dodd S.W., Wood J.F., Whitlow M., Snoy P., and Schlom J. Construction, binding properties, metabolism, and tumor targeting of a single-chain Fv derived from the pancarcinoma monoclonal antibody CC49. Cancer Research 51 (1991) 6363-6371
    • (1991) Cancer Research , vol.51 , pp. 6363-6371
    • Milenic, D.E.1    Yokota, T.2    Filpula, D.R.3    Finkelman, M.A.J.4    Dodd, S.W.5    Wood, J.F.6    Whitlow, M.7    Snoy, P.8    Schlom, J.9
  • 81
    • 22244486057 scopus 로고    scopus 로고
    • Production, purification and characterization of human scFv antibodies expressed in Saccharomyces cerevisiae, Pichia pastoris, and Escherichia coli
    • Miller K.D., Weaver-Feldhaus J., Gray S.A., Siegel R.W., and Feldhaus M.J. Production, purification and characterization of human scFv antibodies expressed in Saccharomyces cerevisiae, Pichia pastoris, and Escherichia coli. Protein Expression and Purification 42 (2005) 255-267
    • (2005) Protein Expression and Purification , vol.42 , pp. 255-267
    • Miller, K.D.1    Weaver-Feldhaus, J.2    Gray, S.A.3    Siegel, R.W.4    Feldhaus, M.J.5
  • 83
    • 0030965970 scopus 로고    scopus 로고
    • Disrupting the hydrophobic patches at the antibody variable/constant domain interface: improved in vivo folding and physical characterization of an engineered scFv fragment
    • Nieba L., Honegger A., Krebber C., and Pluckthun A. Disrupting the hydrophobic patches at the antibody variable/constant domain interface: improved in vivo folding and physical characterization of an engineered scFv fragment. Protein Engineering 10 (1997) 435-444
    • (1997) Protein Engineering , vol.10 , pp. 435-444
    • Nieba, L.1    Honegger, A.2    Krebber, C.3    Pluckthun, A.4
  • 85
    • 0036806997 scopus 로고    scopus 로고
    • Fluorophor-linked immunosorbent assay: a time- and cost-saving method for the characterization of antibody fragments using a fusion protein of a single-chain antibody fragment and enhanced green fluorescent protein
    • Oelschlaeger P., Srikant-Iyer S., Lange S., Schmitt J., and Schmid R.D. Fluorophor-linked immunosorbent assay: a time- and cost-saving method for the characterization of antibody fragments using a fusion protein of a single-chain antibody fragment and enhanced green fluorescent protein. Analytical Biochemistry 309 (2002) 27-34
    • (2002) Analytical Biochemistry , vol.309 , pp. 27-34
    • Oelschlaeger, P.1    Srikant-Iyer, S.2    Lange, S.3    Schmitt, J.4    Schmid, R.D.5
  • 86
    • 14744306329 scopus 로고
    • Synthesis of a functional antiphytochrome single-chain-Fv protein in transgenic tobacco
    • Owen M., Gandecha A., Cockburn B., and Whitelam G. Synthesis of a functional antiphytochrome single-chain-Fv protein in transgenic tobacco. Bio-technology 10 (1992) 790-794
    • (1992) Bio-technology , vol.10 , pp. 790-794
    • Owen, M.1    Gandecha, A.2    Cockburn, B.3    Whitelam, G.4
  • 87
    • 0029347117 scopus 로고
    • Multicopy overexpression of bovine pancreatic trypsin inhibitor saturates the protein folding and secretory capacity of Saccharomyces cerevisiae
    • Parekh R., Forrester K., and Wittrup D. Multicopy overexpression of bovine pancreatic trypsin inhibitor saturates the protein folding and secretory capacity of Saccharomyces cerevisiae. Protein Expression and Purification 6 (1995) 537-545
    • (1995) Protein Expression and Purification , vol.6 , pp. 537-545
    • Parekh, R.1    Forrester, K.2    Wittrup, D.3
  • 90
    • 0032029523 scopus 로고    scopus 로고
    • Genetic engineering of a single-chain antibody fragment for surface immobilization in an optical biosensor
    • Piervincenzi R.T., Reichert W.M., and Hellinga H.W. Genetic engineering of a single-chain antibody fragment for surface immobilization in an optical biosensor. Biosensors and Bioelectronics 13 (1998) 305-312
    • (1998) Biosensors and Bioelectronics , vol.13 , pp. 305-312
    • Piervincenzi, R.T.1    Reichert, W.M.2    Hellinga, H.W.3
  • 91
    • 0029068068 scopus 로고
    • Functional antibody single-chain fragments from the cytoplasm of Escherichia coli: influence of thioredoxin reductase (TrxB)
    • Proba K., Ge L., and Pluckthun A. Functional antibody single-chain fragments from the cytoplasm of Escherichia coli: influence of thioredoxin reductase (TrxB). Gene 159 (1995) 203-207
    • (1995) Gene , vol.159 , pp. 203-207
    • Proba, K.1    Ge, L.2    Pluckthun, A.3
  • 92
    • 0344813702 scopus 로고    scopus 로고
    • Antibody scFv fragments without disulphide bonds made by molecular evolution
    • Proba K., Worn A., Honegger A., and Pluckthun A. Antibody scFv fragments without disulphide bonds made by molecular evolution. Journal of Molecular Biology 275 (1998) 245-253
    • (1998) Journal of Molecular Biology , vol.275 , pp. 245-253
    • Proba, K.1    Worn, A.2    Honegger, A.3    Pluckthun, A.4
  • 95
    • 0028335616 scopus 로고
    • Stabilisation of the Fv fragments in recombinant immunotoxins by disulphide bonds engineered into conserved framework regions
    • Reiter Y., Brinkmann U., Webber K.O., Jung S.H., Lee B., and Pastan I. Stabilisation of the Fv fragments in recombinant immunotoxins by disulphide bonds engineered into conserved framework regions. Biochemistry 33 (1994) 5451-5459
    • (1994) Biochemistry , vol.33 , pp. 5451-5459
    • Reiter, Y.1    Brinkmann, U.2    Webber, K.O.3    Jung, S.H.4    Lee, B.5    Pastan, I.6
  • 96
    • 0028944846 scopus 로고
    • Generation of rabbit monoclonal antibody fragments from a combinatorial phage display library and their production in the yeast Pichia pastoris
    • Ridder R., Schmitx R., Legay F., and Gram H. Generation of rabbit monoclonal antibody fragments from a combinatorial phage display library and their production in the yeast Pichia pastoris. BioTechnology 13 (1995) 255-260
    • (1995) BioTechnology , vol.13 , pp. 255-260
    • Ridder, R.1    Schmitx, R.2    Legay, F.3    Gram, H.4
  • 97
  • 98
    • 0031766998 scopus 로고    scopus 로고
    • Procaryotic expression of single-chain variable-fragment (scFv) antibodies: secretion in L-form cells of Proteus mirabilis leads to active product and overcomes the limitations of periplasmic expression in Escherichia coli
    • Rippmann J.F., Klein M., Hoischen C., Brocks B., Rettig W.J., Gumpert J., Pfizenmaier K., Mattes R., and Moosmayer D. Procaryotic expression of single-chain variable-fragment (scFv) antibodies: secretion in L-form cells of Proteus mirabilis leads to active product and overcomes the limitations of periplasmic expression in Escherichia coli. Applied and Environmental Microbiology 64 (1998) 4862-4869
    • (1998) Applied and Environmental Microbiology , vol.64 , pp. 4862-4869
    • Rippmann, J.F.1    Klein, M.2    Hoischen, C.3    Brocks, B.4    Rettig, W.J.5    Gumpert, J.6    Pfizenmaier, K.7    Mattes, R.8    Moosmayer, D.9
  • 102
    • 0345712326 scopus 로고    scopus 로고
    • High cytoplasmic expression in E-coli, purification, and in vitro refolding of a single chain Fv antibody fragment against the hepatitis B surface antigen
    • Sanchez L., Ayala M., Freyre F., Pedroso I., Bell H., Falcon V., and Gavilondo J.V. High cytoplasmic expression in E-coli, purification, and in vitro refolding of a single chain Fv antibody fragment against the hepatitis B surface antigen. Journal of Biotechnology 72 (1999) 13-20
    • (1999) Journal of Biotechnology , vol.72 , pp. 13-20
    • Sanchez, L.1    Ayala, M.2    Freyre, F.3    Pedroso, I.4    Bell, H.5    Falcon, V.6    Gavilondo, J.V.7
  • 107
    • 0031879861 scopus 로고    scopus 로고
    • Increasing the secretory capacity of Saccharomyces cerevisiae for production of single-chain antibody fragments
    • Shusta E.V., Raines R.T., Pluckthun A., and Wittrup K.D. Increasing the secretory capacity of Saccharomyces cerevisiae for production of single-chain antibody fragments. Nature Biotechnology 16 (1998) 773-777
    • (1998) Nature Biotechnology , vol.16 , pp. 773-777
    • Shusta, E.V.1    Raines, R.T.2    Pluckthun, A.3    Wittrup, K.D.4
  • 109
    • 0036425175 scopus 로고    scopus 로고
    • Rapid refolding and polishing of single chain antibodies from Escherichia coli inclusion bodies
    • Sinacola J.R., and Robinson A.S. Rapid refolding and polishing of single chain antibodies from Escherichia coli inclusion bodies. Protein Expression and Purification 26 (2002) 301-308
    • (2002) Protein Expression and Purification , vol.26 , pp. 301-308
    • Sinacola, J.R.1    Robinson, A.S.2
  • 110
    • 0027312336 scopus 로고
    • Bacteria expression of immunoglobulin fractions
    • Skerra A. Bacteria expression of immunoglobulin fractions. Current Opinion in Immunology 5 (1993) 256-262
    • (1993) Current Opinion in Immunology , vol.5 , pp. 256-262
    • Skerra, A.1
  • 111
    • 0024292736 scopus 로고
    • Assembly of a functional immunoglobulin Fv fragment in Escherichia coli
    • Skerra A., and Pluckthun A. Assembly of a functional immunoglobulin Fv fragment in Escherichia coli. Science 240 (1988) 1038-1041
    • (1988) Science , vol.240 , pp. 1038-1041
    • Skerra, A.1    Pluckthun, A.2
  • 112
    • 10444232073 scopus 로고    scopus 로고
    • Broad-host-range plasmid pJB658 can be used for industrial-level production of a secreted host-toxic single-chain antibody fragment in Escherichia coli
    • Sletta H., Nedal A., Aune T.E.V., Hakvag S., Aune R., Ellingsen T.E., Valla S., and Brautaset T. Broad-host-range plasmid pJB658 can be used for industrial-level production of a secreted host-toxic single-chain antibody fragment in Escherichia coli. Applied and Environmental Microbiology 70 (2004) 7033-7039
    • (2004) Applied and Environmental Microbiology , vol.70 , pp. 7033-7039
    • Sletta, H.1    Nedal, A.2    Aune, T.E.V.3    Hakvag, S.4    Aune, R.5    Ellingsen, T.E.6    Valla, S.7    Brautaset, T.8
  • 113
    • 0037200928 scopus 로고    scopus 로고
    • Overexpression of an archaeal protein in yeast: secretion bottleneck at the ER
    • Smith J.D., and Robinson A.S. Overexpression of an archaeal protein in yeast: secretion bottleneck at the ER. Biotechnology and Bioengineering 79 (2002) 713-723
    • (2002) Biotechnology and Bioengineering , vol.79 , pp. 713-723
    • Smith, J.D.1    Robinson, A.S.2
  • 114
    • 0030476535 scopus 로고    scopus 로고
    • Antibody production in plants
    • Smith M.D. Antibody production in plants. Biotechnology Advances 14 (1996) 267-281
    • (1996) Biotechnology Advances , vol.14 , pp. 267-281
    • Smith, M.D.1
  • 115
    • 0034879260 scopus 로고    scopus 로고
    • Factors affecting the production of a single-chain antibody fragment by Aspergillus awamori in a stirred tank reactor
    • Sotiriadis A., and Keshavarz-Moore E. Factors affecting the production of a single-chain antibody fragment by Aspergillus awamori in a stirred tank reactor. Biotechnology Progress 17 (2001) 618-623
    • (2001) Biotechnology Progress , vol.17 , pp. 618-623
    • Sotiriadis, A.1    Keshavarz-Moore, E.2
  • 116
    • 0027501259 scopus 로고
    • Targeting of T lymphocytes to Nue HER2-expressing cells using chimeric single chain Fv receptors
    • Stancovski I., Schindler D.G., Waks T., Yarden Y., Sela M., and Eshhar Z. Targeting of T lymphocytes to Nue HER2-expressing cells using chimeric single chain Fv receptors. Journal of Immunology 151 (1993) 6577-6582
    • (1993) Journal of Immunology , vol.151 , pp. 6577-6582
    • Stancovski, I.1    Schindler, D.G.2    Waks, T.3    Yarden, Y.4    Sela, M.5    Eshhar, Z.6
  • 117
    • 0025026141 scopus 로고
    • A bifunctional fusion protein containing Fc-binding fragment B of staphylococcal protein A amino terminal to antidigoxin single-chain Fv
    • Tai M.S., Mudgett-Hunter M., Levinson D., Wu G.M., Haber E., Oppermann H., and Hustaon J.S. A bifunctional fusion protein containing Fc-binding fragment B of staphylococcal protein A amino terminal to antidigoxin single-chain Fv. Biochemistry 29 (1990) 8024-8030
    • (1990) Biochemistry , vol.29 , pp. 8024-8030
    • Tai, M.S.1    Mudgett-Hunter, M.2    Levinson, D.3    Wu, G.M.4    Haber, E.5    Oppermann, H.6    Hustaon, J.S.7
  • 120
    • 33645055376 scopus 로고    scopus 로고
    • Targeting of HIV-1 Tat traffic and function by transduction-competent single chain antibodies
    • Theisen D.M., Pongratz C., Wiegmann K., Rivero F., Krut O., and Kronke M. Targeting of HIV-1 Tat traffic and function by transduction-competent single chain antibodies. Vaccine 24 (2006) 3127-3136
    • (2006) Vaccine , vol.24 , pp. 3127-3136
    • Theisen, D.M.1    Pongratz, C.2    Wiegmann, K.3    Rivero, F.4    Krut, O.5    Kronke, M.6
  • 121
    • 10044227272 scopus 로고    scopus 로고
    • Reduced oxygen supply increases process stability and product yield with recombinant Pichia pastoris
    • Trentmann O., Khatri N.K., and Hoffmann F. Reduced oxygen supply increases process stability and product yield with recombinant Pichia pastoris. Biotechnology Progress 20 (2004) 1766-1775
    • (2004) Biotechnology Progress , vol.20 , pp. 1766-1775
    • Trentmann, O.1    Khatri, N.K.2    Hoffmann, F.3
  • 122
    • 0345276454 scopus 로고    scopus 로고
    • Optimization of codon pair use within the (GGGGS)3 linker sequence results in enhanced protein expression
    • Trinh R., Gurbaxani B., Morrison S.L., and Seyfzadeh M. Optimization of codon pair use within the (GGGGS)3 linker sequence results in enhanced protein expression. Molecular Immunology 40 (2004) 717-722
    • (2004) Molecular Immunology , vol.40 , pp. 717-722
    • Trinh, R.1    Gurbaxani, B.2    Morrison, S.L.3    Seyfzadeh, M.4
  • 124
    • 0032122306 scopus 로고    scopus 로고
    • Antibody engineering: comparison of bacterial, yeast, insect and mammalian expression systems
    • Verma R., Boleti E., and George A.J.T. Antibody engineering: comparison of bacterial, yeast, insect and mammalian expression systems. Journal of Immunological Methods 216 (1998) 165-181
    • (1998) Journal of Immunological Methods , vol.216 , pp. 165-181
    • Verma, R.1    Boleti, E.2    George, A.J.T.3
  • 126
    • 0024461313 scopus 로고
    • Binding activities of a repertoire of single immunoglobulin variable domains secreted from Escherichia coli
    • Ward E.S., Gussow D., Griffiths A.D., Jones P.T., and Winter G. Binding activities of a repertoire of single immunoglobulin variable domains secreted from Escherichia coli. Nature 341 (1989) 544-546
    • (1989) Nature , vol.341 , pp. 544-546
    • Ward, E.S.1    Gussow, D.2    Griffiths, A.D.3    Jones, P.T.4    Winter, G.5
  • 128
    • 0024149641 scopus 로고
    • The immunoglobulin superfamily, domains for cell surface recognition
    • Williams A.F., and Barclay A.N. The immunoglobulin superfamily, domains for cell surface recognition. Annual Review of Immunology 6 (1988) 381-405
    • (1988) Annual Review of Immunology , vol.6 , pp. 381-405
    • Williams, A.F.1    Barclay, A.N.2
  • 129
    • 17644386898 scopus 로고    scopus 로고
    • A random peptide library fused to CCR5 for selection of mimetopes expressed on the mammalian cell surface via retroviral vectors
    • Wolkowicz R., Jager G.C., and Nolan G.P. A random peptide library fused to CCR5 for selection of mimetopes expressed on the mammalian cell surface via retroviral vectors. Journal of Biological Chemistry 280 (2005) 15195-15201
    • (2005) Journal of Biological Chemistry , vol.280 , pp. 15195-15201
    • Wolkowicz, R.1    Jager, G.C.2    Nolan, G.P.3
  • 130
    • 0032524034 scopus 로고    scopus 로고
    • An intrinsically stable antibody scFv fragment can tolerate the loss of both disulphide bonds and fold correctly
    • Worn A., and Pluckthun A. An intrinsically stable antibody scFv fragment can tolerate the loss of both disulphide bonds and fold correctly. FEBS Letters 237 (1998) 357-361
    • (1998) FEBS Letters , vol.237 , pp. 357-361
    • Worn, A.1    Pluckthun, A.2
  • 131
    • 0035793208 scopus 로고    scopus 로고
    • Stability engineering of antibody single-chain Fv fragments
    • Worn A., and Pluckthun A. Stability engineering of antibody single-chain Fv fragments. Journal of Molecular Biology 305 (2001) 989-1010
    • (2001) Journal of Molecular Biology , vol.305 , pp. 989-1010
    • Worn, A.1    Pluckthun, A.2
  • 132
    • 0038423087 scopus 로고    scopus 로고
    • Correlation between in vitro stability and in vivo performance of anti-GCN4 intrabodies as cytoplasmic inhibitors
    • Worn A., Auf der Maur A., Escher D., Honegger A., Barberis A., and Pluckthun A. Correlation between in vitro stability and in vivo performance of anti-GCN4 intrabodies as cytoplasmic inhibitors. Journal of Biological Chemistry 275 (2000) 2795-2803
    • (2000) Journal of Biological Chemistry , vol.275 , pp. 2795-2803
    • Worn, A.1    Auf der Maur, A.2    Escher, D.3    Honegger, A.4    Barberis, A.5    Pluckthun, A.6
  • 134
    • 0036307716 scopus 로고    scopus 로고
    • Functional production and characterization of a fibrin-specific single-chain antibody-fragment from Bacillus subtilitis: effects of molecular chaperones and a wall-bound protease on antibody fragment production
    • Wu S.C., Yeung J.C., Duan Y., Ye R., Szarka S.J., Habibi H.R., and Wong S.L. Functional production and characterization of a fibrin-specific single-chain antibody-fragment from Bacillus subtilitis: effects of molecular chaperones and a wall-bound protease on antibody fragment production. Applied and Environmental Microbiology 68 (2002) 3261-3269
    • (2002) Applied and Environmental Microbiology , vol.68 , pp. 3261-3269
    • Wu, S.C.1    Yeung, J.C.2    Duan, Y.3    Ye, R.4    Szarka, S.J.5    Habibi, H.R.6    Wong, S.L.7
  • 135
    • 0028286019 scopus 로고
    • Protein folding in the periplasm of Escherichia coli
    • Wulfing C., and Pluckthun A. Protein folding in the periplasm of Escherichia coli. Molecular Microbiology 12 (1994) 685-692
    • (1994) Molecular Microbiology , vol.12 , pp. 685-692
    • Wulfing, C.1    Pluckthun, A.2
  • 136
    • 24044505375 scopus 로고    scopus 로고
    • Analysis of unfolded protein response during single-chain antibody expression in Saccharomyces cerevisiae reveals different roles for BiP and PDI in folding
    • Xu P., Doyle III F.J., and Robinson A.S. Analysis of unfolded protein response during single-chain antibody expression in Saccharomyces cerevisiae reveals different roles for BiP and PDI in folding. Metabolic Engineering 7 (2005) 269-279
    • (2005) Metabolic Engineering , vol.7 , pp. 269-279
    • Xu, P.1    Doyle III, F.J.2    Robinson, A.S.3
  • 137
    • 0026684815 scopus 로고
    • Rapid tumour penetration of a single-chain Fv and comparison with other immunoglobulin forms
    • Yokota T., Milenic D.E., Whitlow M., and Schlom J. Rapid tumour penetration of a single-chain Fv and comparison with other immunoglobulin forms. Cancer Research 52 (1992) 3402-3408
    • (1992) Cancer Research , vol.52 , pp. 3402-3408
    • Yokota, T.1    Milenic, D.E.2    Whitlow, M.3    Schlom, J.4
  • 138
    • 0029557830 scopus 로고
    • Thermal stabilization of a single-chain Fv antibody fragment by introduction of a disulphide bond
    • Young N.M., MacKenzie C.R., Narang S.A., Oomen R.P., and Baenziger J.E. Thermal stabilization of a single-chain Fv antibody fragment by introduction of a disulphide bond. FEBS Letters 377 (1995) 135-139
    • (1995) FEBS Letters , vol.377 , pp. 135-139
    • Young, N.M.1    MacKenzie, C.R.2    Narang, S.A.3    Oomen, R.P.4    Baenziger, J.E.5
  • 139
    • 0038308559 scopus 로고    scopus 로고
    • Production of a functional catalytic antibody ScFv-NusA fusion protein in bacterial cytoplasm
    • Zheng L., Baumann U., and Reymond J.L. Production of a functional catalytic antibody ScFv-NusA fusion protein in bacterial cytoplasm. Journal of Biochemistry (Tokyo) 133 (2003) 577-581
    • (2003) Journal of Biochemistry (Tokyo) , vol.133 , pp. 577-581
    • Zheng, L.1    Baumann, U.2    Reymond, J.L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.