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Volumn 17, Issue 4, 2007, Pages 467-473

Yeast surface display for protein engineering and characterization

Author keywords

[No Author keywords available]

Indexed keywords

ENZYME; EPITOPE; PROTEIN;

EID: 34648832245     PISSN: 0959440X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.sbi.2007.08.012     Document Type: Review
Times cited : (317)

References (65)
  • 1
    • 0030994634 scopus 로고    scopus 로고
    • Yeast surface display for screening combinatorial polypeptide libraries
    • Boder E.T., and Wittrup K.D. Yeast surface display for screening combinatorial polypeptide libraries. Nat Biotechnol 15 (1997) 553-557
    • (1997) Nat Biotechnol , vol.15 , pp. 553-557
    • Boder, E.T.1    Wittrup, K.D.2
  • 2
    • 34247176809 scopus 로고    scopus 로고
    • Isolating and engineering human antibodies using yeast surface display
    • This paper provides a detailed and comprehensive protocol for engineering proteins by yeast surface display. While the focus is on isolating and engineering scFvs, the procedures are applicable for engineering any protein that can be displayed by yeast and whose binding target is available in soluble form.
    • Chao G., Lau W.L., Hackel B.J., Sazinsky S.L., Lippow S.M., and Wittrup K.D. Isolating and engineering human antibodies using yeast surface display. Nat Protoc 1 (2006) 755-768. This paper provides a detailed and comprehensive protocol for engineering proteins by yeast surface display. While the focus is on isolating and engineering scFvs, the procedures are applicable for engineering any protein that can be displayed by yeast and whose binding target is available in soluble form.
    • (2006) Nat Protoc , vol.1 , pp. 755-768
    • Chao, G.1    Lau, W.L.2    Hackel, B.J.3    Sazinsky, S.L.4    Lippow, S.M.5    Wittrup, K.D.6
  • 3
    • 33947155314 scopus 로고    scopus 로고
    • Antigen selection from an HIV-1 immune antibody library displayed on yeast yields many novel antibodies compared to selection from the same library displayed on phage
    • This study offers the first direct comparison of yeast surface display and phage display. From identical libraries, screened with the same antigen, yeast display was found to identify many more high-affinity clones and also required less effort. These two significant advantages of yeast display were attributed to, respectively, eukaryotic processing and flow-cytometry-based library screening and clone analysis.
    • Bowley D.R., Labrijn A.F., Zwick M.B., and Burton D.R. Antigen selection from an HIV-1 immune antibody library displayed on yeast yields many novel antibodies compared to selection from the same library displayed on phage. Protein Eng Des Sel 20 (2007) 81-90. This study offers the first direct comparison of yeast surface display and phage display. From identical libraries, screened with the same antigen, yeast display was found to identify many more high-affinity clones and also required less effort. These two significant advantages of yeast display were attributed to, respectively, eukaryotic processing and flow-cytometry-based library screening and clone analysis.
    • (2007) Protein Eng Des Sel , vol.20 , pp. 81-90
    • Bowley, D.R.1    Labrijn, A.F.2    Zwick, M.B.3    Burton, D.R.4
  • 4
    • 33645467944 scopus 로고    scopus 로고
    • Construction and application of a yeast surface-displayed human cDNA library to identify post-translational modification-dependent protein-protein interactions
    • Bidlingmaier S., and Liu B. Construction and application of a yeast surface-displayed human cDNA library to identify post-translational modification-dependent protein-protein interactions. Mol Cell Proteomics 5 (2006) 533-540
    • (2006) Mol Cell Proteomics , vol.5 , pp. 533-540
    • Bidlingmaier, S.1    Liu, B.2
  • 8
    • 33745219391 scopus 로고    scopus 로고
    • Construction and characterization of a pseudo-immune human antibody library using yeast surface display
    • Lee H.-W., Lee S.-H., Park K.-J., Kim J.-S., Kwon M.-H., and Kim Y.-S. Construction and characterization of a pseudo-immune human antibody library using yeast surface display. Biochem Biophys Res Commun 346 (2006) 896-903
    • (2006) Biochem Biophys Res Commun , vol.346 , pp. 896-903
    • Lee, H.-W.1    Lee, S.-H.2    Park, K.-J.3    Kim, J.-S.4    Kwon, M.-H.5    Kim, Y.-S.6
  • 9
    • 33751420234 scopus 로고    scopus 로고
    • Method for generation of in vivo biotinylated recombinant antibodies by yeast mating
    • Scholler N., Garvik B., Quarles T., Jiang S., and Urban N. Method for generation of in vivo biotinylated recombinant antibodies by yeast mating. J Immunol Methods 317 (2006) 132-143
    • (2006) J Immunol Methods , vol.317 , pp. 132-143
    • Scholler, N.1    Garvik, B.2    Quarles, T.3    Jiang, S.4    Urban, N.5
  • 10
    • 27544483522 scopus 로고    scopus 로고
    • Directed evolution for the development of conformation-specific affinity reagents using yeast display
    • Weaver-Feldhaus J.M., Miller K.D., Feldhaus M.J., and Siegel R.W. Directed evolution for the development of conformation-specific affinity reagents using yeast display. Protein Eng Des Sel 18 (2005) 527-536
    • (2005) Protein Eng Des Sel , vol.18 , pp. 527-536
    • Weaver-Feldhaus, J.M.1    Miller, K.D.2    Feldhaus, M.J.3    Siegel, R.W.4
  • 11
    • 33947424302 scopus 로고    scopus 로고
    • Mining a yeast library for brain endothelial cell-binding antibodies
    • Wang X.X., Cho Y.K., and Shusta E.V. Mining a yeast library for brain endothelial cell-binding antibodies. Nat Methods 4 (2007) 143-145
    • (2007) Nat Methods , vol.4 , pp. 143-145
    • Wang, X.X.1    Cho, Y.K.2    Shusta, E.V.3
  • 12
    • 23144436953 scopus 로고    scopus 로고
    • Probing the interface between biomolecules and inorganic materials using yeast surface display and genetic engineering
    • Peelle B.R., Krauland E.M., Wittrup K.D., and Belcher A.M. Probing the interface between biomolecules and inorganic materials using yeast surface display and genetic engineering. Acta Biomater 1 (2005) 145-154
    • (2005) Acta Biomater , vol.1 , pp. 145-154
    • Peelle, B.R.1    Krauland, E.M.2    Wittrup, K.D.3    Belcher, A.M.4
  • 14
    • 34347337714 scopus 로고    scopus 로고
    • Improvement of a recombinant anti-monkey anti-CD3 diphtheria toxin based immunotoxin by yeast display affinity maturation of the scFv
    • Wang Z., Kim G.-B., Woo J.-H., Liu Y.Y., Mathias A., Stavrou S., and Neville D.M. Improvement of a recombinant anti-monkey anti-CD3 diphtheria toxin based immunotoxin by yeast display affinity maturation of the scFv. Bioconjugate Chem 18 (2007) 947-955
    • (2007) Bioconjugate Chem , vol.18 , pp. 947-955
    • Wang, Z.1    Kim, G.-B.2    Woo, J.-H.3    Liu, Y.Y.4    Mathias, A.5    Stavrou, S.6    Neville, D.M.7
  • 16
    • 33846138044 scopus 로고    scopus 로고
    • Molecular evolution of antibody cross-reactivity for two subtypes of type A botulinum neurotoxin
    • This study illustrates the use of yeast surface display for selectively expanding antibody reactivity. Starting from a scFv that recognizes botulinum neurotoxin type A1 with high affinity, the authors identified a mutant that recognizes type A2 with high affinity as well. Notably, the selection process required independent and simultaneous quantification of binding to both target antigens, which was enabled by cell-surface display and flow cytometry.
    • Garcia-Rodriguez C., Levy R., Arndt J.W., Forsyth C.M., Razai A., Lou J., Geren I., Stevens R.C., and Marks J.D. Molecular evolution of antibody cross-reactivity for two subtypes of type A botulinum neurotoxin. Nat Biotechnol 25 (2007) 107-116. This study illustrates the use of yeast surface display for selectively expanding antibody reactivity. Starting from a scFv that recognizes botulinum neurotoxin type A1 with high affinity, the authors identified a mutant that recognizes type A2 with high affinity as well. Notably, the selection process required independent and simultaneous quantification of binding to both target antigens, which was enabled by cell-surface display and flow cytometry.
    • (2007) Nat Biotechnol , vol.25 , pp. 107-116
    • Garcia-Rodriguez, C.1    Levy, R.2    Arndt, J.W.3    Forsyth, C.M.4    Razai, A.5    Lou, J.6    Geren, I.7    Stevens, R.C.8    Marks, J.D.9
  • 17
    • 34249852867 scopus 로고    scopus 로고
    • High-affinity single-domain binding proteins with a binary-code interface
    • In this work, fibronectin scaffold binders with only tyrosine and serine in their variable loops were identified by first screening a phage-displayed library, followed by a yeast-displayed library for fine affinity discrimination.
    • Koide A., Gilbreth R.N., Esaki K., Tereshko V., and Koide S. High-affinity single-domain binding proteins with a binary-code interface. Proc Natl Acad Sci USA 104 (2007) 6632-6637. In this work, fibronectin scaffold binders with only tyrosine and serine in their variable loops were identified by first screening a phage-displayed library, followed by a yeast-displayed library for fine affinity discrimination.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 6632-6637
    • Koide, A.1    Gilbreth, R.N.2    Esaki, K.3    Tereshko, V.4    Koide, S.5
  • 18
    • 34247098240 scopus 로고    scopus 로고
    • Evolution of an interloop disulfide bond in high-affinity antibody mimics based on fibronectin type III domain and selected by yeast surface display: molecular convergence with single-domain camelid and shark antibodies
    • Lipovsek D., Lippow S.M., Hackel B.J., Gregson M.W., Cheng P., Kapila A., and Wittrup K.D. Evolution of an interloop disulfide bond in high-affinity antibody mimics based on fibronectin type III domain and selected by yeast surface display: molecular convergence with single-domain camelid and shark antibodies. J Mol Biol 368 (2007) 1024-1041
    • (2007) J Mol Biol , vol.368 , pp. 1024-1041
    • Lipovsek, D.1    Lippow, S.M.2    Hackel, B.J.3    Gregson, M.W.4    Cheng, P.5    Kapila, A.6    Wittrup, K.D.7
  • 20
    • 33745726188 scopus 로고    scopus 로고
    • Improved mutants from directed evolution are biased to orthologous substitutions
    • Cochran J.R., Kim Y.-S., Lippow S.M., Rao B., and Wittrup K.D. Improved mutants from directed evolution are biased to orthologous substitutions. Protein Eng Des Sel 19 (2006) 245-253
    • (2006) Protein Eng Des Sel , vol.19 , pp. 245-253
    • Cochran, J.R.1    Kim, Y.-S.2    Lippow, S.M.3    Rao, B.4    Wittrup, K.D.5
  • 21
    • 25144479800 scopus 로고    scopus 로고
    • Characterization of T cell receptors engineered for high affinity against toxic shock syndrome toxin-1
    • Buonpane R.A., Moza B., Sundberg E.J., and Kranz D.M. Characterization of T cell receptors engineered for high affinity against toxic shock syndrome toxin-1. J Mol Biol 353 (2005) 308-321
    • (2005) J Mol Biol , vol.353 , pp. 308-321
    • Buonpane, R.A.1    Moza, B.2    Sundberg, E.J.3    Kranz, D.M.4
  • 22
    • 30044449525 scopus 로고    scopus 로고
    • Class II-restricted T cell receptor engineered in vitro for higher affinity retains peptide specificity and function
    • In this study, a panel of higher-affinity mutants of a class II-restricted TCR was generated, found to retain exquisite peptide specificity, and used to address the functional consequences of TCR affinity on T cell activation.
    • Weber K.S., Donermeyer D.L., Allen P.M., and Kranz D.M. Class II-restricted T cell receptor engineered in vitro for higher affinity retains peptide specificity and function. Proc Natl Acad Sci USA 102 (2005) 19033-19038. In this study, a panel of higher-affinity mutants of a class II-restricted TCR was generated, found to retain exquisite peptide specificity, and used to address the functional consequences of TCR affinity on T cell activation.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 19033-19038
    • Weber, K.S.1    Donermeyer, D.L.2    Allen, P.M.3    Kranz, D.M.4
  • 23
    • 34250000045 scopus 로고    scopus 로고
    • Neutralization of staphylococcal enterotoxin B by soluble, high-affinity receptor antagonists
    • This study describes the affinity maturation of a TCR V domain against the superantigen staphylococcal enterotoxin B (SEB). A mutant possessing a three-million-fold increase in binding affinity was isolated and found to potently antagonize lethal SEB activity in animal models.
    • Buonpane R.A., Churchill H.R.O., Moza B., Sundberg E.J., Peterson M.L., Schlievert P.M., and Kranz D.M. Neutralization of staphylococcal enterotoxin B by soluble, high-affinity receptor antagonists. Nat Med 13 (2007) 725-729. This study describes the affinity maturation of a TCR V domain against the superantigen staphylococcal enterotoxin B (SEB). A mutant possessing a three-million-fold increase in binding affinity was isolated and found to potently antagonize lethal SEB activity in animal models.
    • (2007) Nat Med , vol.13 , pp. 725-729
    • Buonpane, R.A.1    Churchill, H.R.O.2    Moza, B.3    Sundberg, E.J.4    Peterson, M.L.5    Schlievert, P.M.6    Kranz, D.M.7
  • 24
    • 0033536626 scopus 로고    scopus 로고
    • Yeast polypeptide fusion surface display levels predict thermal stability and soluble secretion efficiency
    • Shusta E.V., Kieke M.C., Parke E., Kranz D.M., and Wittrup K.D. Yeast polypeptide fusion surface display levels predict thermal stability and soluble secretion efficiency. J Mol Biol 292 (1999) 949-956
    • (1999) J Mol Biol , vol.292 , pp. 949-956
    • Shusta, E.V.1    Kieke, M.C.2    Parke, E.3    Kranz, D.M.4    Wittrup, K.D.5
  • 27
    • 33644846817 scopus 로고    scopus 로고
    • Directed evolution of the epidermal growth factor receptor extracellular domain for expression in yeast
    • Kim Y.-S., Bhandari R., Cochran J.R., Kuriyan J., and Wittrup K.D. Directed evolution of the epidermal growth factor receptor extracellular domain for expression in yeast. Proteins Struct Funct Bioinformatics 62 (2006) 1026-1035
    • (2006) Proteins Struct Funct Bioinformatics , vol.62 , pp. 1026-1035
    • Kim, Y.-S.1    Bhandari, R.2    Cochran, J.R.3    Kuriyan, J.4    Wittrup, K.D.5
  • 28
    • 33646250654 scopus 로고    scopus 로고
    • Limitations of yeast surface display in engineering proteins of high thermostability
    • Park S., Xu Y., Stowell X.F., Gai F., Saven J.G., and Boder E.T. Limitations of yeast surface display in engineering proteins of high thermostability. Protein Eng Des Sel 19 (2006) 211-217
    • (2006) Protein Eng Des Sel , vol.19 , pp. 211-217
    • Park, S.1    Xu, Y.2    Stowell, X.F.3    Gai, F.4    Saven, J.G.5    Boder, E.T.6
  • 29
    • 33847181688 scopus 로고    scopus 로고
    • A novel high-throughput screen reveals yeast genes that increase secretion of heterologous proteins
    • Wentz A.E., and Shusta E.V. A novel high-throughput screen reveals yeast genes that increase secretion of heterologous proteins. Appl Environ Microbiol 73 (2007) 1189-1198
    • (2007) Appl Environ Microbiol , vol.73 , pp. 1189-1198
    • Wentz, A.E.1    Shusta, E.V.2
  • 30
    • 33747180836 scopus 로고    scopus 로고
    • A flow cytometric assay for screening improved heterologous protein secretion in yeast
    • Rakestraw J.A., Baskaran A.R., and Wittrup K.D. A flow cytometric assay for screening improved heterologous protein secretion in yeast. Biotechnol Prog 22 (2006) 1200-1208
    • (2006) Biotechnol Prog , vol.22 , pp. 1200-1208
    • Rakestraw, J.A.1    Baskaran, A.R.2    Wittrup, K.D.3
  • 31
    • 4344589735 scopus 로고    scopus 로고
    • Fine epitope mapping of anti-epidermal growth factor receptor antibodies through random mutagenesis and yeast surface display
    • This study details the application of yeast surface display for identifying key residues mediating protein-protein interactions. By constructing a library of randomly mutagenized EGFR variants and screening with anti-EGFR antibodies, the authors mapped the binding epitopes of these antibodies with residue resolution. Significantly, this technique identifies discontinuous and heat-denaturable epitopes, samples substitutions to amino acids other than alanine, and requires no soluble expression and purification of mutants.
    • Chao G., Cochran J.R., and Dane Wittrup K. Fine epitope mapping of anti-epidermal growth factor receptor antibodies through random mutagenesis and yeast surface display. J Mol Biol 342 (2004) 539-550. This study details the application of yeast surface display for identifying key residues mediating protein-protein interactions. By constructing a library of randomly mutagenized EGFR variants and screening with anti-EGFR antibodies, the authors mapped the binding epitopes of these antibodies with residue resolution. Significantly, this technique identifies discontinuous and heat-denaturable epitopes, samples substitutions to amino acids other than alanine, and requires no soluble expression and purification of mutants.
    • (2004) J Mol Biol , vol.342 , pp. 539-550
    • Chao, G.1    Cochran, J.R.2    Dane Wittrup, K.3
  • 32
    • 21044448356 scopus 로고    scopus 로고
    • Development of a humanized monoclonal antibody with therapeutic potential against West Nile Virus
    • This study applies yeast surface display for determining the antigenic epitopes recognized by a panel of monoclonal antibodies specific for the envelope protein of West Nile Virus. Significantly, the epitope map of antibody E16 has been validated by crystallographic data, presented in Nybakken et al.
    • Oliphant T., Engle M., Nybakken G.E., Doane C., Johnson S., Huang L., Gorlatov S., Mehlhop E., Marri A., Chung K.M., et al. Development of a humanized monoclonal antibody with therapeutic potential against West Nile Virus. Nat Med 11 (2005) 522-530. This study applies yeast surface display for determining the antigenic epitopes recognized by a panel of monoclonal antibodies specific for the envelope protein of West Nile Virus. Significantly, the epitope map of antibody E16 has been validated by crystallographic data, presented in Nybakken et al.
    • (2005) Nat Med , vol.11 , pp. 522-530
    • Oliphant, T.1    Engle, M.2    Nybakken, G.E.3    Doane, C.4    Johnson, S.5    Huang, L.6    Gorlatov, S.7    Mehlhop, E.8    Marri, A.9    Chung, K.M.10
  • 33
  • 36
    • 31144442443 scopus 로고    scopus 로고
    • Antibodies against West Nile Virus nonstructural protein NS1 prevent lethal infection through Fc γ receptor-dependent and -independent mechanisms
    • Chung K.M., Nybakken G.E., Thompson B.S., Engle M.J., Marri A., Fremont D.H., and Diamond M.S. Antibodies against West Nile Virus nonstructural protein NS1 prevent lethal infection through Fc γ receptor-dependent and -independent mechanisms. J Virol 80 (2006) 1340-1351
    • (2006) J Virol , vol.80 , pp. 1340-1351
    • Chung, K.M.1    Nybakken, G.E.2    Thompson, B.S.3    Engle, M.J.4    Marri, A.5    Fremont, D.H.6    Diamond, M.S.7
  • 37
    • 33751546855 scopus 로고    scopus 로고
    • Fine and domain-level epitope mapping of botulinum neurotoxin type A neutralizing antibodies by yeast surface display
    • Levy R., Forsyth C.M., LaPorte S.L., Geren I.N., Smith L.A., and Marks J.D. Fine and domain-level epitope mapping of botulinum neurotoxin type A neutralizing antibodies by yeast surface display. J Mol Biol 365 (2007) 196-210
    • (2007) J Mol Biol , vol.365 , pp. 196-210
    • Levy, R.1    Forsyth, C.M.2    LaPorte, S.L.3    Geren, I.N.4    Smith, L.A.5    Marks, J.D.6
  • 39
    • 23044477106 scopus 로고    scopus 로고
    • Comprehensive antibody epitope mapping of the nucleocapsid protein of severe acute respiratory syndrome (SARS) coronavirus: insight into the humoral immunity of SARS
    • Liang Y., Wan Y., Qiu L.-W., Zhou J., Ni B., Guo B., Zou Q., Zou L., Zhou W., Jia Z., et al. Comprehensive antibody epitope mapping of the nucleocapsid protein of severe acute respiratory syndrome (SARS) coronavirus: insight into the humoral immunity of SARS. Clin Chem 51 (2005) 1382-1396
    • (2005) Clin Chem , vol.51 , pp. 1382-1396
    • Liang, Y.1    Wan, Y.2    Qiu, L.-W.3    Zhou, J.4    Ni, B.5    Guo, B.6    Zou, Q.7    Zou, L.8    Zhou, W.9    Jia, Z.10
  • 40
    • 24344500862 scopus 로고    scopus 로고
    • The use of scFv-displaying yeast in mammalian cell surface selections
    • This study describes a method for screening yeast-displayed libraries by monolayer panning, which is well suited for engineering of proteins whose binding targets are not readily solubilized and expressed by adherent cells.
    • Wang X.X., and Shusta E.V. The use of scFv-displaying yeast in mammalian cell surface selections. J Immunol Methods 304 (2005) 30-42. This study describes a method for screening yeast-displayed libraries by monolayer panning, which is well suited for engineering of proteins whose binding targets are not readily solubilized and expressed by adherent cells.
    • (2005) J Immunol Methods , vol.304 , pp. 30-42
    • Wang, X.X.1    Shusta, E.V.2
  • 41
    • 33745698185 scopus 로고    scopus 로고
    • Development of a novel strategy for engineering high-affinity proteins by yeast display
    • This study describes a method for screening yeast-displayed libraries by density centrifugation, which is well suited for engineering proteins whose binding targets are not readily solubilized and expressed by cells grown in suspension.
    • Richman S.A., Healan S.J., Weber K.S., Donermeyer D.L., Dossett M.L., Greenberg P.D., Allen P.M., and Kranz D.M. Development of a novel strategy for engineering high-affinity proteins by yeast display. Protein Eng Des Sel 19 (2006) 255-264. This study describes a method for screening yeast-displayed libraries by density centrifugation, which is well suited for engineering proteins whose binding targets are not readily solubilized and expressed by cells grown in suspension.
    • (2006) Protein Eng Des Sel , vol.19 , pp. 255-264
    • Richman, S.A.1    Healan, S.J.2    Weber, K.S.3    Donermeyer, D.L.4    Dossett, M.L.5    Greenberg, P.D.6    Allen, P.M.7    Kranz, D.M.8
  • 42
    • 23144455709 scopus 로고    scopus 로고
    • Design criteria for engineering inorganic material-specific peptides
    • Peelle B.R., Krauland E.M., Wittrup K.D., and Belcher A.M. Design criteria for engineering inorganic material-specific peptides. Langmuir 21 (2005) 6929-6933
    • (2005) Langmuir , vol.21 , pp. 6929-6933
    • Peelle, B.R.1    Krauland, E.M.2    Wittrup, K.D.3    Belcher, A.M.4
  • 43
    • 34547583175 scopus 로고    scopus 로고
    • Krauland EM, Peelle BR, Wittrup KD, Belcher AM: Peptide tags for enhanced cellular and protein adhesion to single-crystalline sapphire. Biotechnol Bioeng 2007:n/a.
  • 44
    • 33645211498 scopus 로고    scopus 로고
    • Effective display of metallothionein tandem repeats on the bioadsorption of cadmium ion
    • Kuroda K., and Ueda M. Effective display of metallothionein tandem repeats on the bioadsorption of cadmium ion. Appl Microbiol Biotechnol 70 (2006) 458-463
    • (2006) Appl Microbiol Biotechnol , vol.70 , pp. 458-463
    • Kuroda, K.1    Ueda, M.2
  • 45
    • 33747163289 scopus 로고    scopus 로고
    • Development of novel yeast cell surface display system for homo-oligomeric protein by coexpression of native and anchored subunits
    • Furukawa H., Tanino T., Fukuda H., and Kondo A. Development of novel yeast cell surface display system for homo-oligomeric protein by coexpression of native and anchored subunits. Biotechnol Prog 22 (2006) 994-997
    • (2006) Biotechnol Prog , vol.22 , pp. 994-997
    • Furukawa, H.1    Tanino, T.2    Fukuda, H.3    Kondo, A.4
  • 46
    • 34547405733 scopus 로고    scopus 로고
    • Construction of a novel synergistic system for production and recovery of secreted recombinant proteins by the cell surface engineering
    • Shibasaki S., Kawabata A., Ishii J., Yagi S., Kadonosono T., Kato M., Fukuda N., Kondo A., and Ueda M. Construction of a novel synergistic system for production and recovery of secreted recombinant proteins by the cell surface engineering. Appl Microbiol Biotechnol 75 (2007) 821-828
    • (2007) Appl Microbiol Biotechnol , vol.75 , pp. 821-828
    • Shibasaki, S.1    Kawabata, A.2    Ishii, J.3    Yagi, S.4    Kadonosono, T.5    Kato, M.6    Fukuda, N.7    Kondo, A.8    Ueda, M.9
  • 47
  • 48
    • 33746847277 scopus 로고    scopus 로고
    • The surface display of haemolysin from vibrio harveyi on yeast cells and their potential applications as live vaccine in marine fish
    • Zhu K., Chi Z., Li J., Zhang F., Li M., Yasoda H.N., and Wu L. The surface display of haemolysin from vibrio harveyi on yeast cells and their potential applications as live vaccine in marine fish. Vaccine 24 (2006) 6046-6052
    • (2006) Vaccine , vol.24 , pp. 6046-6052
    • Zhu, K.1    Chi, Z.2    Li, J.3    Zhang, F.4    Li, M.5    Yasoda, H.N.6    Wu, L.7
  • 49
    • 33747198499 scopus 로고    scopus 로고
    • Application of the arming system for the expression of the 380R antigen from Red Sea Bream Iridovirus (RSIV) on the surface of yeast cells: a first step for the development of an oral vaccine
    • Tamaru Y., Ohtsuka M., Kato K., Manabe S., Kuroda K., Sanada M., and Ueda M. Application of the arming system for the expression of the 380R antigen from Red Sea Bream Iridovirus (RSIV) on the surface of yeast cells: a first step for the development of an oral vaccine. Biotechnol Prog 22 (2006) 949-953
    • (2006) Biotechnol Prog , vol.22 , pp. 949-953
    • Tamaru, Y.1    Ohtsuka, M.2    Kato, K.3    Manabe, S.4    Kuroda, K.5    Sanada, M.6    Ueda, M.7
  • 51
    • 23744488193 scopus 로고    scopus 로고
    • Enhanced reactivity of Rhizopus oryzae lipase displayed on yeast cell surfaces in organic solvents: potential as a whole-cell biocatalyst in organic solvents
    • Shiraga S., Kawakami M., Ishiguro M., and Ueda M. Enhanced reactivity of Rhizopus oryzae lipase displayed on yeast cell surfaces in organic solvents: potential as a whole-cell biocatalyst in organic solvents. Appl Environ Microbiol 71 (2005) 4335-4338
    • (2005) Appl Environ Microbiol , vol.71 , pp. 4335-4338
    • Shiraga, S.1    Kawakami, M.2    Ishiguro, M.3    Ueda, M.4
  • 52
    • 27544481402 scopus 로고    scopus 로고
    • Creation of Rhizopus oryzae lipase having a unique oxyanion hole by combinatorial mutagenesis in the lid domain
    • Shiraga S., Ishiguro M., Fukami H., Nakao M., and Ueda M. Creation of Rhizopus oryzae lipase having a unique oxyanion hole by combinatorial mutagenesis in the lid domain. Appl Microbiol Biotechnol 68 (2005) 779-785
    • (2005) Appl Microbiol Biotechnol , vol.68 , pp. 779-785
    • Shiraga, S.1    Ishiguro, M.2    Fukami, H.3    Nakao, M.4    Ueda, M.5
  • 53
    • 28844499786 scopus 로고    scopus 로고
    • An immobilized biotin ligase: surface display of Escherichia coli BirA on Saccharomyces cerevisiae
    • Parthasarathy R., Bajaj J., and Boder E.T. An immobilized biotin ligase: surface display of Escherichia coli BirA on Saccharomyces cerevisiae. Biotechnol Prog 21 (2005) 1627-1631
    • (2005) Biotechnol Prog , vol.21 , pp. 1627-1631
    • Parthasarathy, R.1    Bajaj, J.2    Boder, E.T.3
  • 55
    • 33750969690 scopus 로고    scopus 로고
    • Cell surface expression of bacterial esterase a by Saccharomyces cerevisiae and its enhancement by constitutive activation of the cellular unfolded protein response
    • Breinig F., Diehl B., Rau S., Zimmer C., Schwab H., and Schmitt M.J. Cell surface expression of bacterial esterase a by Saccharomyces cerevisiae and its enhancement by constitutive activation of the cellular unfolded protein response. Appl Environ Microbiol 72 (2006) 7140-7147
    • (2006) Appl Environ Microbiol , vol.72 , pp. 7140-7147
    • Breinig, F.1    Diehl, B.2    Rau, S.3    Zimmer, C.4    Schwab, H.5    Schmitt, M.J.6
  • 57
    • 34250722034 scopus 로고    scopus 로고
    • Improved bread-baking process using Saccharomyces cerevisiae displayed with engineered cyclodextrin glucanotransferase
    • Shim J.-H., Seo N.-S., Roh S.-A., Kim J.-W., Cha H., and Park K.-H. Improved bread-baking process using Saccharomyces cerevisiae displayed with engineered cyclodextrin glucanotransferase. J Agric Food Chem 55 (2007) 4735-4740
    • (2007) J Agric Food Chem , vol.55 , pp. 4735-4740
    • Shim, J.-H.1    Seo, N.-S.2    Roh, S.-A.3    Kim, J.-W.4    Cha, H.5    Park, K.-H.6
  • 58
    • 34250852934 scopus 로고    scopus 로고
    • Metallopeptidase, neurolysin, as a novel molecular tool for analysis of properties of cancer-producing matrix metalloproteinases-2 and -9
    • Kadonosono T., Kato M., and Ueda M. Metallopeptidase, neurolysin, as a novel molecular tool for analysis of properties of cancer-producing matrix metalloproteinases-2 and -9. Appl Microbiol Biotechnol 75 (2007) 1285-1291
    • (2007) Appl Microbiol Biotechnol , vol.75 , pp. 1285-1291
    • Kadonosono, T.1    Kato, M.2    Ueda, M.3
  • 59
    • 33745464891 scopus 로고    scopus 로고
    • Isolation of anti-CD22 Fv with high affinity by Fv display on human cells
    • Ho M., Nagata S., and Pastan I. Isolation of anti-CD22 Fv with high affinity by Fv display on human cells. Proc Natl Acad Sci USA 103 (2006) 9637-9642
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 9637-9642
    • Ho, M.1    Nagata, S.2    Pastan, I.3
  • 61
    • 23244440386 scopus 로고    scopus 로고
    • High-affinity CD25-binding IL-2 mutants potently stimulate persistent T cell growth
    • Rao B.M., Driver I., Lauffenburger D.A., and Wittrup K.D. High-affinity CD25-binding IL-2 mutants potently stimulate persistent T cell growth. Biochemistry 44 (2005) 10696-10701
    • (2005) Biochemistry , vol.44 , pp. 10696-10701
    • Rao, B.M.1    Driver, I.2    Lauffenburger, D.A.3    Wittrup, K.D.4
  • 62
    • 0034718615 scopus 로고    scopus 로고
    • Directed evolution of antibody fragments with monovalent femtomolar antigen-binding affinity
    • Boder E.T., Midelfort K.S., and Wittrup K.D. Directed evolution of antibody fragments with monovalent femtomolar antigen-binding affinity. Proc Natl Acad Sci USA 97 (2000) 10701-10705
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 10701-10705
    • Boder, E.T.1    Midelfort, K.S.2    Wittrup, K.D.3
  • 63
    • 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. Biotechnol Prog 21 (2005) 349-357
    • (2005) Biotechnol Prog , vol.21 , pp. 349-357
    • Huang, D.1    Shusta, E.V.2
  • 64
    • 28444457689 scopus 로고    scopus 로고
    • Yeast surface display of a noncovalent MHC class II heterodimer complexed with antigenic peptide
    • Boder E.T., Bill J.R., Nields A.W., Marrack P.C., and Kappler J.W. Yeast surface display of a noncovalent MHC class II heterodimer complexed with antigenic peptide. Biotechnol Bioeng 92 (2005) 485-491
    • (2005) Biotechnol Bioeng , vol.92 , pp. 485-491
    • Boder, E.T.1    Bill, J.R.2    Nields, A.W.3    Marrack, P.C.4    Kappler, J.W.5
  • 65
    • 0031473847 scopus 로고    scopus 로고
    • Swiss-model and the swiss-pdbviewer: an environment for comparative protein modeling
    • Guex N., and Peitsch M.C. Swiss-model and the swiss-pdbviewer: an environment for comparative protein modeling. Electrophoresis 18 (1997) 2714-2723
    • (1997) Electrophoresis , vol.18 , pp. 2714-2723
    • Guex, N.1    Peitsch, M.C.2


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