메뉴 건너뛰기




Volumn 13, Issue 7-8, 2008, Pages 318-324

Screening isolates from antibody phage-display libraries

Author keywords

[No Author keywords available]

Indexed keywords

ANTIBODY;

EID: 41549099541     PISSN: 13596446     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.drudis.2007.10.012     Document Type: Review
Times cited : (32)

References (73)
  • 1
    • 0025226085 scopus 로고
    • Phage antibodies: filamentous phage displaying antibody variable domains
    • McCafferty J., et al. Phage antibodies: filamentous phage displaying antibody variable domains. Nature 348 (1990) 552-554
    • (1990) Nature , vol.348 , pp. 552-554
    • McCafferty, J.1
  • 2
    • 33846324426 scopus 로고    scopus 로고
    • Synthetic antibodies as therapeutics
    • Fuh G. Synthetic antibodies as therapeutics. Expert Opin. Biol. Ther. 7 (2007) 73-87
    • (2007) Expert Opin. Biol. Ther. , vol.7 , pp. 73-87
    • Fuh, G.1
  • 3
    • 3142743794 scopus 로고    scopus 로고
    • Antibodies from phage antibody libraries
    • Bradbury A.R., and Marks J.D. Antibodies from phage antibody libraries. J. Immunol. Methods 290 (2004) 29-49
    • (2004) J. Immunol. Methods , vol.290 , pp. 29-49
    • Bradbury, A.R.1    Marks, J.D.2
  • 4
    • 27144431943 scopus 로고    scopus 로고
    • Selecting and screening recombinant antibody libraries
    • Hoogenboom H.R. Selecting and screening recombinant antibody libraries. Nat. Biotechnol. 23 (2005) 1105-1116
    • (2005) Nat. Biotechnol. , vol.23 , pp. 1105-1116
    • Hoogenboom, H.R.1
  • 5
    • 0028141993 scopus 로고
    • Guiding the selection of human antibodies from phage display repertoires to a single epitope of an antigen
    • Jespers L.S., et al. Guiding the selection of human antibodies from phage display repertoires to a single epitope of an antigen. Biotechnology (N Y) 12 (1994) 899-903
    • (1994) Biotechnology (N Y) , vol.12 , pp. 899-903
    • Jespers, L.S.1
  • 6
    • 17644406997 scopus 로고    scopus 로고
    • From rodent reagents to human therapeutics using antibody guided selection
    • Osbourn J., et al. From rodent reagents to human therapeutics using antibody guided selection. Methods 36 (2005) 61-68
    • (2005) Methods , vol.36 , pp. 61-68
    • Osbourn, J.1
  • 7
    • 27144457667 scopus 로고    scopus 로고
    • Monoclonal antibody successes in the clinic
    • Reichert J.M., et al. Monoclonal antibody successes in the clinic. Nat. Biotechnol. 23 (2005) 1073-1078
    • (2005) Nat. Biotechnol. , vol.23 , pp. 1073-1078
    • Reichert, J.M.1
  • 8
    • 33746163862 scopus 로고    scopus 로고
    • Biopharmaceutical benchmarks 2006
    • Walsh G. Biopharmaceutical benchmarks 2006. Nat. Biotechnol. 24 (2006) 769-776
    • (2006) Nat. Biotechnol. , vol.24 , pp. 769-776
    • Walsh, G.1
  • 9
    • 33646352962 scopus 로고    scopus 로고
    • Potent antibody therapeutics by design
    • Carter P.J. Potent antibody therapeutics by design. Nat. Rev. Immunol. 6 (2006) 343-357
    • (2006) Nat. Rev. Immunol. , vol.6 , pp. 343-357
    • Carter, P.J.1
  • 10
    • 28444488346 scopus 로고    scopus 로고
    • Filamentous phage display in the new millennium
    • Kehoe J.W., and Kay B.K. Filamentous phage display in the new millennium. Chem. Rev. 105 (2005) 4056-4072
    • (2005) Chem. Rev. , vol.105 , pp. 4056-4072
    • Kehoe, J.W.1    Kay, B.K.2
  • 11
    • 15344339459 scopus 로고    scopus 로고
    • Considerations on antibody-phage display methodology
    • Conrad U., and Scheller J. Considerations on antibody-phage display methodology. Comb. Chem. High Throughput Screen 8 (2005) 117-126
    • (2005) Comb. Chem. High Throughput Screen , vol.8 , pp. 117-126
    • Conrad, U.1    Scheller, J.2
  • 12
    • 0026317443 scopus 로고
    • By-passing immunization. Human antibodies from V-gene libraries displayed on phage
    • Marks J.D., et al. By-passing immunization. Human antibodies from V-gene libraries displayed on phage. J. Mol. Biol. 222 (1991) 581-597
    • (1991) J. Mol. Biol. , vol.222 , pp. 581-597
    • Marks, J.D.1
  • 13
    • 0025740577 scopus 로고
    • Multi-subunit proteins on the surface of filamentous phage: methodologies for displaying antibody (Fab) heavy and light chains
    • Hoogenboom H.R., et al. Multi-subunit proteins on the surface of filamentous phage: methodologies for displaying antibody (Fab) heavy and light chains. Nucleic Acids Res. 19 (1991) 4133-4137
    • (1991) Nucleic Acids Res. , vol.19 , pp. 4133-4137
    • Hoogenboom, H.R.1
  • 14
    • 13144261717 scopus 로고    scopus 로고
    • Efficient construction of a large nonimmune phage antibody library: the production of high-affinity human single-chain antibodies to protein antigens
    • Sheets M.D., et al. Efficient construction of a large nonimmune phage antibody library: the production of high-affinity human single-chain antibodies to protein antigens. Proc. Natl. Acad. Sci. U. S. A. 95 (1998) 6157-6162
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , pp. 6157-6162
    • Sheets, M.D.1
  • 15
    • 9344223986 scopus 로고    scopus 로고
    • Human antibodies with sub-nanomolar affinities isolated from a large non-immunized phage display library
    • Vaughan T.J., et al. Human antibodies with sub-nanomolar affinities isolated from a large non-immunized phage display library. Nat. Biotechnol. 14 (1996) 309-314
    • (1996) Nat. Biotechnol. , vol.14 , pp. 309-314
    • Vaughan, T.J.1
  • 16
    • 0033603596 scopus 로고    scopus 로고
    • A large non-immunized human Fab fragment phage library that permits rapid isolation and kinetic analysis of high affinity antibodies
    • de Haard H.J., et al. A large non-immunized human Fab fragment phage library that permits rapid isolation and kinetic analysis of high affinity antibodies. J. Biol. Chem. 274 (1999) 18218-18230
    • (1999) J. Biol. Chem. , vol.274 , pp. 18218-18230
    • de Haard, H.J.1
  • 17
    • 0037391745 scopus 로고    scopus 로고
    • Recombinant antibodies for cancer diagnosis and therapy
    • Souriau C., and Hudson P.J. Recombinant antibodies for cancer diagnosis and therapy. Expert Opin. Biol. Ther. 3 (2003) 305-318
    • (2003) Expert Opin. Biol. Ther. , vol.3 , pp. 305-318
    • Souriau, C.1    Hudson, P.J.2
  • 18
    • 0034635335 scopus 로고    scopus 로고
    • Fully synthetic human combinatorial antibody libraries (HuCAL) based on modular consensus frameworks and CDRs randomized with trinucleotides
    • Knappik A., et al. Fully synthetic human combinatorial antibody libraries (HuCAL) based on modular consensus frameworks and CDRs randomized with trinucleotides. J. Mol. Biol. 296 (2000) 57-86
    • (2000) J. Mol. Biol. , vol.296 , pp. 57-86
    • Knappik, A.1
  • 19
    • 1842609526 scopus 로고    scopus 로고
    • Phage-displayed antibody libraries of synthetic heavy chain complementarity determining regions
    • Sidhu S.S., et al. Phage-displayed antibody libraries of synthetic heavy chain complementarity determining regions. J. Mol. Biol. 338 (2004) 299-310
    • (2004) J. Mol. Biol. , vol.338 , pp. 299-310
    • Sidhu, S.S.1
  • 20
    • 0141866900 scopus 로고    scopus 로고
    • Human combinatorial Fab library yielding specific and functional antibodies against the human fibroblast growth factor receptor 3
    • Rauchenberger R., et al. Human combinatorial Fab library yielding specific and functional antibodies against the human fibroblast growth factor receptor 3. J. Biol. Chem. 278 (2003) 38194-38205
    • (2003) J. Biol. Chem. , vol.278 , pp. 38194-38205
    • Rauchenberger, R.1
  • 21
    • 21444439732 scopus 로고    scopus 로고
    • Generation of high-affinity human antibodies by combining donor-derived and synthetic complementarity-determining-region diversity
    • Hoet R.M., et al. Generation of high-affinity human antibodies by combining donor-derived and synthetic complementarity-determining-region diversity. Nat. Biotechnol. 23 (2005) 344-348
    • (2005) Nat. Biotechnol. , vol.23 , pp. 344-348
    • Hoet, R.M.1
  • 22
    • 0026641471 scopus 로고
    • Molecular evolution of proteins on filamentous phage. Mimicking the strategy of the immune system
    • Marks J.D., et al. Molecular evolution of proteins on filamentous phage. Mimicking the strategy of the immune system. J. Biol. Chem. 267 (1992) 16007-16010
    • (1992) J. Biol. Chem. , vol.267 , pp. 16007-16010
    • Marks, J.D.1
  • 23
    • 0026699293 scopus 로고
    • Selection of phage antibodies by binding affinity. Mimicking affinity maturation
    • Hawkins R.E., et al. Selection of phage antibodies by binding affinity. Mimicking affinity maturation. J. Mol. Biol. 226 (1992) 889-896
    • (1992) J. Mol. Biol. , vol.226 , pp. 889-896
    • Hawkins, R.E.1
  • 24
    • 0034425742 scopus 로고    scopus 로고
    • Antibody arrays for high-throughput screening of antibody-antigen interactions
    • de Wildt R.M., et al. Antibody arrays for high-throughput screening of antibody-antigen interactions. Nat. Biotechnol. 18 (2000) 989-994
    • (2000) Nat. Biotechnol. , vol.18 , pp. 989-994
    • de Wildt, R.M.1
  • 25
    • 0036303521 scopus 로고    scopus 로고
    • Towards proteome-wide production of monoclonal antibody by phage display
    • Liu B., et al. Towards proteome-wide production of monoclonal antibody by phage display. J. Mol. Biol. 315 (2002) 1063-1073
    • (2002) J. Mol. Biol. , vol.315 , pp. 1063-1073
    • Liu, B.1
  • 26
    • 0025190770 scopus 로고
    • A single-step procedure for cloning and selection of antibody-secreting hybridomas
    • Gherardi E., et al. A single-step procedure for cloning and selection of antibody-secreting hybridomas. J. Immunol. Methods 126 (1990) 61-68
    • (1990) J. Immunol. Methods , vol.126 , pp. 61-68
    • Gherardi, E.1
  • 27
    • 0025825576 scopus 로고
    • Colony assays for antibody fragments expressed in bacteria
    • Dreher M.L., et al. Colony assays for antibody fragments expressed in bacteria. J. Immunol. Methods 139 (1991) 197-205
    • (1991) J. Immunol. Methods , vol.139 , pp. 197-205
    • Dreher, M.L.1
  • 28
    • 0025783791 scopus 로고
    • Filter screening of antibody Fab fragments secreted from individual bacterial colonies: specific detection of antigen binding with a two-membrane system
    • Skerra A., et al. Filter screening of antibody Fab fragments secreted from individual bacterial colonies: specific detection of antigen binding with a two-membrane system. Anal. Biochem. 196 (1991) 151-155
    • (1991) Anal. Biochem. , vol.196 , pp. 151-155
    • Skerra, A.1
  • 29
    • 0032519481 scopus 로고    scopus 로고
    • Discovery of human antibodies to cell surface antigens by capture lift screening of phage-expressed antibody libraries
    • Watkins J.D., et al. Discovery of human antibodies to cell surface antigens by capture lift screening of phage-expressed antibody libraries. Anal. Biochem. 256 (1998) 169-177
    • (1998) Anal. Biochem. , vol.256 , pp. 169-177
    • Watkins, J.D.1
  • 30
    • 0036124397 scopus 로고    scopus 로고
    • Cloning, isolation and characterization of human tumor in situ monoclonal antibodies
    • Wu H., et al. Cloning, isolation and characterization of human tumor in situ monoclonal antibodies. Cancer Immunol. Immunother. 51 (2002) 79-90
    • (2002) Cancer Immunol. Immunother. , vol.51 , pp. 79-90
    • Wu, H.1
  • 31
    • 0035290720 scopus 로고    scopus 로고
    • Isolation of anti-angiogenesis antibodies from a large combinatorial repertoire by colony filter screening
    • Giovannoni L., et al. Isolation of anti-angiogenesis antibodies from a large combinatorial repertoire by colony filter screening. Nucleic Acids Res. 29 (2001) E27
    • (2001) Nucleic Acids Res. , vol.29
    • Giovannoni, L.1
  • 32
    • 0032555478 scopus 로고    scopus 로고
    • Design and use of a phage display library. Human antibodies with subnanomolar affinity against a marker of angiogenesis eluted from a two-dimensional gel
    • Pini A., et al. Design and use of a phage display library. Human antibodies with subnanomolar affinity against a marker of angiogenesis eluted from a two-dimensional gel. J. Biol. Chem. 273 (1998) 21769-21776
    • (1998) J. Biol. Chem. , vol.273 , pp. 21769-21776
    • Pini, A.1
  • 33
    • 0037253089 scopus 로고    scopus 로고
    • Protein arrays: the current state-of-the-art
    • Cutler P. Protein arrays: the current state-of-the-art. Proteomics 3 (2003) 3-18
    • (2003) Proteomics , vol.3 , pp. 3-18
    • Cutler, P.1
  • 34
    • 33744811399 scopus 로고    scopus 로고
    • Microarray technology as a universal tool for high-throughput analysis of biological systems
    • Sobek J., et al. Microarray technology as a universal tool for high-throughput analysis of biological systems. Comb. Chem. High Throughput Screen 9 (2006) 365-380
    • (2006) Comb. Chem. High Throughput Screen , vol.9 , pp. 365-380
    • Sobek, J.1
  • 35
    • 33846288924 scopus 로고    scopus 로고
    • Multiplexing molecular diagnostics and immunoassays using emerging microarray technologies
    • Ling M.M., et al. Multiplexing molecular diagnostics and immunoassays using emerging microarray technologies. Expert Rev. Mol. Diagn. 7 (2007) 87-98
    • (2007) Expert Rev. Mol. Diagn. , vol.7 , pp. 87-98
    • Ling, M.M.1
  • 36
    • 3142773316 scopus 로고    scopus 로고
    • Multiplexed sandwich assays in microarray format
    • Nielsen U.B., and Geierstanger B.H. Multiplexed sandwich assays in microarray format. J. Immunol. Methods 290 (2004) 107-120
    • (2004) J. Immunol. Methods , vol.290 , pp. 107-120
    • Nielsen, U.B.1    Geierstanger, B.H.2
  • 37
    • 33747063065 scopus 로고    scopus 로고
    • Comparison of random and oriented immobilisation of antibody fragments on mixed self-assembled monolayers
    • Bonroy K., et al. Comparison of random and oriented immobilisation of antibody fragments on mixed self-assembled monolayers. J. Immunol. Methods 312 (2006) 167-181
    • (2006) J. Immunol. Methods , vol.312 , pp. 167-181
    • Bonroy, K.1
  • 38
    • 0037439369 scopus 로고    scopus 로고
    • Optimizing antibody immobilization strategies for the construction of protein microarrays
    • Peluso P., et al. Optimizing antibody immobilization strategies for the construction of protein microarrays. Anal. Biochem. 312 (2003) 113-124
    • (2003) Anal. Biochem. , vol.312 , pp. 113-124
    • Peluso, P.1
  • 39
    • 0032983924 scopus 로고    scopus 로고
    • In vivo biotinylated recombinant antibodies: high efficiency of labelling and application to the cloning of active anti-human IgG1 Fab fragments
    • Sibler A.P., et al. In vivo biotinylated recombinant antibodies: high efficiency of labelling and application to the cloning of active anti-human IgG1 Fab fragments. J. Immunol. Methods 224 (1999) 129-140
    • (1999) J. Immunol. Methods , vol.224 , pp. 129-140
    • Sibler, A.P.1
  • 40
    • 0032212036 scopus 로고    scopus 로고
    • In vitro enzymatic biotinylation of recombinant fab fragments through a peptide acceptor tail
    • Saviranta P., et al. In vitro enzymatic biotinylation of recombinant fab fragments through a peptide acceptor tail. Bioconjug. Chem. 9 (1998) 725-735
    • (1998) Bioconjug. Chem. , vol.9 , pp. 725-735
    • Saviranta, P.1
  • 41
    • 0032881726 scopus 로고    scopus 로고
    • High-throughput microarray-based enzyme-linked immunosorbent assay (ELISA)
    • 782-776, 788
    • Mendoza L.G., et al. High-throughput microarray-based enzyme-linked immunosorbent assay (ELISA). Biotechniques 27 (1999) 778-780 782-776, 788
    • (1999) Biotechniques , vol.27 , pp. 778-780
    • Mendoza, L.G.1
  • 42
    • 0347297217 scopus 로고    scopus 로고
    • Microarray of recombinant antibodies using a streptavidin sensor surface self-assembled onto a gold layer
    • Pavlickova P., et al. Microarray of recombinant antibodies using a streptavidin sensor surface self-assembled onto a gold layer. Biotechniques 34 (2003) 124-130
    • (2003) Biotechniques , vol.34 , pp. 124-130
    • Pavlickova, P.1
  • 43
    • 2442647916 scopus 로고    scopus 로고
    • Seeing better through a MIST: evaluation of monoclonal recombinant antibody fragments on microarrays
    • Angenendt P., et al. Seeing better through a MIST: evaluation of monoclonal recombinant antibody fragments on microarrays. Anal. Chem. 76 (2004) 2916-2921
    • (2004) Anal. Chem. , vol.76 , pp. 2916-2921
    • Angenendt, P.1
  • 44
    • 20644459237 scopus 로고    scopus 로고
    • Protein microarrays for antibody profiling: specificity and affinity determination on a chip
    • Poetz O., et al. Protein microarrays for antibody profiling: specificity and affinity determination on a chip. Proteomics 5 (2005) 2402-2411
    • (2005) Proteomics , vol.5 , pp. 2402-2411
    • Poetz, O.1
  • 45
    • 0031032155 scopus 로고    scopus 로고
    • Reliable cloning of functional antibody variable domains from hybridomas and spleen cell repertoires employing a reengineered phage display system
    • Krebber A., et al. Reliable cloning of functional antibody variable domains from hybridomas and spleen cell repertoires employing a reengineered phage display system. J. Immunol. Methods 201 (1997) 35-55
    • (1997) J. Immunol. Methods , vol.201 , pp. 35-55
    • Krebber, A.1
  • 46
    • 33845913565 scopus 로고    scopus 로고
    • A simple vector system to improve performance and utilisation of recombinant antibodies
    • Martin C.D., et al. A simple vector system to improve performance and utilisation of recombinant antibodies. BMC Biotechnol. 6 (2006) 46
    • (2006) BMC Biotechnol. , vol.6 , pp. 46
    • Martin, C.D.1
  • 47
    • 0033152010 scopus 로고    scopus 로고
    • pSKAP/S: An expression vector for the production of single-chain Fv alkaline phosphatase fusion proteins
    • Griep R.A., et al. pSKAP/S: An expression vector for the production of single-chain Fv alkaline phosphatase fusion proteins. Protein Expr. Purif. 16 (1999) 63-69
    • (1999) Protein Expr. Purif. , vol.16 , pp. 63-69
    • Griep, R.A.1
  • 48
    • 1542409973 scopus 로고    scopus 로고
    • Accelerated screening of phage-display output with alkaline phosphatase fusions
    • Han Z., et al. Accelerated screening of phage-display output with alkaline phosphatase fusions. Comb. Chem. High Throughput Screen 7 (2004) 55-62
    • (2004) Comb. Chem. High Throughput Screen , vol.7 , pp. 55-62
    • Han, Z.1
  • 49
    • 0033922052 scopus 로고    scopus 로고
    • Green fluorescent antibodies: novel in vitro tools
    • Casey J.L., et al. Green fluorescent antibodies: novel in vitro tools. Protein Eng. 13 (2000) 445-452
    • (2000) Protein Eng. , vol.13 , pp. 445-452
    • Casey, J.L.1
  • 50
    • 0032758727 scopus 로고    scopus 로고
    • Fluobodies: green fluorescent single-chain Fv fusion proteins
    • Griep R.A., et al. Fluobodies: green fluorescent single-chain Fv fusion proteins. J. Immunol. Methods 230 (1999) 121-130
    • (1999) J. Immunol. Methods , vol.230 , pp. 121-130
    • Griep, R.A.1
  • 51
    • 0034026771 scopus 로고    scopus 로고
    • Production of fluorescent single-chain antibody fragments in Escherichia coli
    • Schwalbach G., et al. Production of fluorescent single-chain antibody fragments in Escherichia coli. Protein Expr. Purif. 18 (2000) 121-132
    • (2000) Protein Expr. Purif. , vol.18 , pp. 121-132
    • Schwalbach, G.1
  • 52
    • 18344374893 scopus 로고    scopus 로고
    • Multiplexed protein profiling on microarrays by rolling-circle amplification
    • Schweitzer B., et al. Multiplexed protein profiling on microarrays by rolling-circle amplification. Nat. Biotechnol. 20 (2002) 359-365
    • (2002) Nat. Biotechnol. , vol.20 , pp. 359-365
    • Schweitzer, B.1
  • 53
    • 0034730034 scopus 로고    scopus 로고
    • Inaugural article: immunoassays with rolling circle DNA amplification: a versatile platform for ultrasensitive antigen detection
    • Schweitzer B., et al. Inaugural article: immunoassays with rolling circle DNA amplification: a versatile platform for ultrasensitive antigen detection. Proc. Natl. Acad. Sci. U. S. A. 97 (2000) 10113-10119
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 10113-10119
    • Schweitzer, B.1
  • 54
    • 33645305964 scopus 로고    scopus 로고
    • High-throughput affinity ranking of antibodies using surface plasmon resonance microarrays
    • Wassaf D., et al. High-throughput affinity ranking of antibodies using surface plasmon resonance microarrays. Anal. Biochem. 351 (2006) 241-253
    • (2006) Anal. Biochem. , vol.351 , pp. 241-253
    • Wassaf, D.1
  • 55
    • 33644867597 scopus 로고    scopus 로고
    • Rapid kinetic-based screening of human Fab fragments
    • Steukers M., et al. Rapid kinetic-based screening of human Fab fragments. J. Immunol. Methods 310 (2006) 126-135
    • (2006) J. Immunol. Methods , vol.310 , pp. 126-135
    • Steukers, M.1
  • 56
    • 0034874270 scopus 로고    scopus 로고
    • Bioassay of prostate-specific antigen (PSA) using microcantilevers
    • Wu G., et al. Bioassay of prostate-specific antigen (PSA) using microcantilevers. Nat. Biotechnol. 19 (2001) 856-860
    • (2001) Nat. Biotechnol. , vol.19 , pp. 856-860
    • Wu, G.1
  • 57
    • 0036230933 scopus 로고    scopus 로고
    • Zeptosens' protein microarrays: a novel high performance microarray platform for low abundance protein analysis
    • Pawlak M., et al. Zeptosens' protein microarrays: a novel high performance microarray platform for low abundance protein analysis. Proteomics 2 (2002) 383-393
    • (2002) Proteomics , vol.2 , pp. 383-393
    • Pawlak, M.1
  • 58
    • 33747278446 scopus 로고    scopus 로고
    • Magnetic acoustic resonance immunoassay (MARIA): a multifrequency acoustic approach for the non-labelled detection of biomolecular interactions
    • Araya-Kleinsteuber B., et al. Magnetic acoustic resonance immunoassay (MARIA): a multifrequency acoustic approach for the non-labelled detection of biomolecular interactions. J. Mol. Recognit. 19 (2006) 379-385
    • (2006) J. Mol. Recognit. , vol.19 , pp. 379-385
    • Araya-Kleinsteuber, B.1
  • 59
    • 0035427605 scopus 로고    scopus 로고
    • High-throughput generation and engineering of recombinant human antibodies
    • Krebs B., et al. High-throughput generation and engineering of recombinant human antibodies. J. Immunol. Methods 254 (2001) 67-84
    • (2001) J. Immunol. Methods , vol.254 , pp. 67-84
    • Krebs, B.1
  • 60
    • 0346908660 scopus 로고    scopus 로고
    • Automation of phage display for high-throughput antibody development
    • Konthur Z., and Walter G. Automation of phage display for high-throughput antibody development. Targets 1 (2002) 30-36
    • (2002) Targets , vol.1 , pp. 30-36
    • Konthur, Z.1    Walter, G.2
  • 61
    • 0036916581 scopus 로고    scopus 로고
    • Automated screening procedure for high-throughput generation of antibody fragments
    • Hallborn J., and Carlsson R. Automated screening procedure for high-throughput generation of antibody fragments. Biotechniques Suppl. (2002) 30-37
    • (2002) Biotechniques , vol.SUPPL , pp. 30-37
    • Hallborn, J.1    Carlsson, R.2
  • 62
    • 0035052057 scopus 로고    scopus 로고
    • High-throughput screening of surface displayed gene products
    • Walter G., et al. High-throughput screening of surface displayed gene products. Comb. Chem. High Throughput Screen 4 (2001) 193-205
    • (2001) Comb. Chem. High Throughput Screen , vol.4 , pp. 193-205
    • Walter, G.1
  • 63
    • 0035048105 scopus 로고    scopus 로고
    • The powerful combination of phage surface display of cDNA libraries and high throughput screening
    • Crameri R., and Kodzius R. The powerful combination of phage surface display of cDNA libraries and high throughput screening. Comb. Chem. High Throughput Screen 4 (2001) 145-155
    • (2001) Comb. Chem. High Throughput Screen , vol.4 , pp. 145-155
    • Crameri, R.1    Kodzius, R.2
  • 64
    • 0142257954 scopus 로고    scopus 로고
    • The remarkable flexibility of the human antibody repertoire; isolation of over one thousand different antibodies to a single protein, BLyS
    • Edwards B.M., et al. The remarkable flexibility of the human antibody repertoire; isolation of over one thousand different antibodies to a single protein, BLyS. J. Mol. Biol. 334 (2003) 103-118
    • (2003) J. Mol. Biol. , vol.334 , pp. 103-118
    • Edwards, B.M.1
  • 65
    • 3242760800 scopus 로고    scopus 로고
    • High-affinity human antibodies from phage-displayed synthetic Fab libraries with a single framework scaffold
    • Lee C.V., et al. High-affinity human antibodies from phage-displayed synthetic Fab libraries with a single framework scaffold. J. Mol. Biol. 340 (2004) 1073-1093
    • (2004) J. Mol. Biol. , vol.340 , pp. 1073-1093
    • Lee, C.V.1
  • 66
    • 33845971497 scopus 로고    scopus 로고
    • Using phage display to select antibodies recognizing post-translational modifications independently of sequence context
    • Kehoe J.W., et al. Using phage display to select antibodies recognizing post-translational modifications independently of sequence context. Mol. Cell Proteomics 5 (2006) 2350-2363
    • (2006) Mol. Cell Proteomics , vol.5 , pp. 2350-2363
    • Kehoe, J.W.1
  • 67
    • 0031281388 scopus 로고    scopus 로고
    • Determination of the relative affinities of antibody fragments expressed in Escherichia coli by enzyme-linked immunosorbent assay
    • Watkins J.D., et al. Determination of the relative affinities of antibody fragments expressed in Escherichia coli by enzyme-linked immunosorbent assay. Anal. Biochem. 253 (1997) 37-45
    • (1997) Anal. Biochem. , vol.253 , pp. 37-45
    • Watkins, J.D.1
  • 68
    • 0034625113 scopus 로고    scopus 로고
    • Crystal structure of a Staphylococcus aureus protein A domain complexed with the Fab fragment of a human IgM antibody: structural basis for recognition of B-cell receptors and superantigen activity
    • Graille M., et al. Crystal structure of a Staphylococcus aureus protein A domain complexed with the Fab fragment of a human IgM antibody: structural basis for recognition of B-cell receptors and superantigen activity. Proc. Natl. Acad. Sci. U. S. A. 97 (2000) 5399-5404
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 5399-5404
    • Graille, M.1
  • 69
    • 0346668339 scopus 로고    scopus 로고
    • Evidence for plasticity and structural mimicry at the immunoglobulin light chain-protein L interface
    • Graille M., et al. Evidence for plasticity and structural mimicry at the immunoglobulin light chain-protein L interface. J. Biol. Chem. 277 (2002) 47500-47506
    • (2002) J. Biol. Chem. , vol.277 , pp. 47500-47506
    • Graille, M.1
  • 70
    • 0035211409 scopus 로고    scopus 로고
    • Recent advances in DNA sequencing by capillary and microdevice electrophoresis
    • Mitnik L., et al. Recent advances in DNA sequencing by capillary and microdevice electrophoresis. Electrophoresis 22 (2001) 4104-4117
    • (2001) Electrophoresis , vol.22 , pp. 4104-4117
    • Mitnik, L.1
  • 71
    • 3142564397 scopus 로고    scopus 로고
    • Rapid generation of functional human IgG antibodies derived from Fab-on-phage display libraries
    • Jostock T., et al. Rapid generation of functional human IgG antibodies derived from Fab-on-phage display libraries. J. Immunol. Methods 289 (2004) 65-80
    • (2004) J. Immunol. Methods , vol.289 , pp. 65-80
    • Jostock, T.1
  • 72
    • 0031978181 scopus 로고    scopus 로고
    • Base-calling of automated sequencer traces using phred. II. Error probabilities
    • Ewing B., and Green P. Base-calling of automated sequencer traces using phred. II. Error probabilities. Genome Res. 8 (1998) 186-194
    • (1998) Genome Res. , vol.8 , pp. 186-194
    • Ewing, B.1    Green, P.2
  • 73
    • 41549083956 scopus 로고    scopus 로고
    • Christiansen, T.O., J; Wall L. (2000) Programming Perl, 3rd Edition. (Book, Publisher: O'Reilly)
    • Christiansen, T.O., J; Wall L. (2000) Programming Perl, 3rd Edition. (Book, Publisher: O'Reilly)


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.