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1
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0030994634
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Yeast surface display for screening combinatorial polypeptide libraries
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Boder E.T., and Wittrup K.D. Yeast surface display for screening combinatorial polypeptide libraries. Nat Biotechnol 15 (1997) 553-557
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(1997)
Nat Biotechnol
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Boder, E.T.1
Wittrup, K.D.2
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2
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34247176809
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Isolating and engineering human antibodies using yeast surface display
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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.
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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.
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Nat Protoc
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Chao, G.1
Lau, W.L.2
Hackel, B.J.3
Sazinsky, S.L.4
Lippow, S.M.5
Wittrup, K.D.6
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3
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33947155314
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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
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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.
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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.
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(2007)
Protein Eng Des Sel
, vol.20
, pp. 81-90
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Bowley, D.R.1
Labrijn, A.F.2
Zwick, M.B.3
Burton, D.R.4
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4
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33645467944
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Construction and application of a yeast surface-displayed human cDNA library to identify post-translational modification-dependent protein-protein interactions
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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
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Mol Cell Proteomics
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Bidlingmaier, S.1
Liu, B.2
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5
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30444454959
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Prospective study on the expression of cancer testis genes and antibody responses in 100 consecutive patients with primary breast cancer
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Mischo A., Kubuschok B., Ertan K., Preuss K.-D., Romeike B., Regitz E., Schormann C., de Bruijn D., Wadle A., Neumann F., et al. Prospective study on the expression of cancer testis genes and antibody responses in 100 consecutive patients with primary breast cancer. Int J Cancer 118 (2006) 696-703
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Int J Cancer
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Mischo, A.1
Kubuschok, B.2
Ertan, K.3
Preuss, K.-D.4
Romeike, B.5
Regitz, E.6
Schormann, C.7
de Bruijn, D.8
Wadle, A.9
Neumann, F.10
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6
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33646530977
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Serological immune response to cancer testis antigens in patients with pancreatic cancer
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Wadle A., Kubuschok B., Imig J., Wüllner B., Wittig C., Zwick C., Mischo A., Wätzig K., Romeike B.F.M., Lindemann W., et al. Serological immune response to cancer testis antigens in patients with pancreatic cancer. Int J Cancer 119 (2006) 117-125
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Int J Cancer
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Wadle, A.1
Kubuschok, B.2
Imig, J.3
Wüllner, B.4
Wittig, C.5
Zwick, C.6
Mischo, A.7
Wätzig, K.8
Romeike, B.F.M.9
Lindemann, W.10
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7
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24344435109
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Serological identification of breast cancer-related antigens from a Saccharomyces cerevisiae surface display library
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Wadle A., Mischo A., Imig J., Wüllner B., Hensel D., Wätzig K., Neumann F., Kubuschok B., Schmidt W., Old L.J., et al. Serological identification of breast cancer-related antigens from a Saccharomyces cerevisiae surface display library. Int J Cancer 117 (2005) 104-113
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Int J Cancer
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Wadle, A.1
Mischo, A.2
Imig, J.3
Wüllner, B.4
Hensel, D.5
Wätzig, K.6
Neumann, F.7
Kubuschok, B.8
Schmidt, W.9
Old, L.J.10
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8
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33745219391
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Construction and characterization of a pseudo-immune human antibody library using yeast surface display
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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
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(2006)
Biochem Biophys Res Commun
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Lee, H.-W.1
Lee, S.-H.2
Park, K.-J.3
Kim, J.-S.4
Kwon, M.-H.5
Kim, Y.-S.6
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9
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33751420234
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Method for generation of in vivo biotinylated recombinant antibodies by yeast mating
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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
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(2006)
J Immunol Methods
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, pp. 132-143
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Scholler, N.1
Garvik, B.2
Quarles, T.3
Jiang, S.4
Urban, N.5
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10
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27544483522
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Directed evolution for the development of conformation-specific affinity reagents using yeast display
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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
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(2005)
Protein Eng Des Sel
, vol.18
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Weaver-Feldhaus, J.M.1
Miller, K.D.2
Feldhaus, M.J.3
Siegel, R.W.4
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11
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33947424302
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Mining a yeast library for brain endothelial cell-binding antibodies
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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
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(2007)
Nat Methods
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, pp. 143-145
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Wang, X.X.1
Cho, Y.K.2
Shusta, E.V.3
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12
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23144436953
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Probing the interface between biomolecules and inorganic materials using yeast surface display and genetic engineering
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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
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(2005)
Acta Biomater
, vol.1
, pp. 145-154
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Peelle, B.R.1
Krauland, E.M.2
Wittrup, K.D.3
Belcher, A.M.4
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13
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20844463814
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A general method for greatly improving the affinity of antibodies by using combinatorial libraries
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Rajpal A., Beyaz N., Haber L., Cappuccilli G., Yee H., Bhatt R.R., Takeuchi T., Lerner R.A., and Crea R. A general method for greatly improving the affinity of antibodies by using combinatorial libraries. Proc Natl Acad Sci USA 102 (2005) 8466-8471
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(2005)
Proc Natl Acad Sci USA
, vol.102
, pp. 8466-8471
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Rajpal, A.1
Beyaz, N.2
Haber, L.3
Cappuccilli, G.4
Yee, H.5
Bhatt, R.R.6
Takeuchi, T.7
Lerner, R.A.8
Crea, R.9
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14
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34347337714
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Improvement of a recombinant anti-monkey anti-CD3 diphtheria toxin based immunotoxin by yeast display affinity maturation of the scFv
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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
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(2007)
Bioconjugate Chem
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, pp. 947-955
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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
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15
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22144473731
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Molecular evolution of antibody affinity for sensitive detection of botulinum neurotoxin type A
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Razai A., Garcia-Rodriguez C., Lou J., Geren I.N., Forsyth C.M., Robles Y., Tsai R., Smith T.J., Smith L.A., Siegel R.W., et al. Molecular evolution of antibody affinity for sensitive detection of botulinum neurotoxin type A. J Mol Biol 351 (2005) 158-169
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(2005)
J Mol Biol
, vol.351
, pp. 158-169
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Razai, A.1
Garcia-Rodriguez, C.2
Lou, J.3
Geren, I.N.4
Forsyth, C.M.5
Robles, Y.6
Tsai, R.7
Smith, T.J.8
Smith, L.A.9
Siegel, R.W.10
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16
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33846138044
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Molecular evolution of antibody cross-reactivity for two subtypes of type A botulinum neurotoxin
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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.
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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.
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(2007)
Nat Biotechnol
, vol.25
, pp. 107-116
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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
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17
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34249852867
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High-affinity single-domain binding proteins with a binary-code interface
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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.
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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.
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(2007)
Proc Natl Acad Sci USA
, vol.104
, pp. 6632-6637
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Koide, A.1
Gilbreth, R.N.2
Esaki, K.3
Tereshko, V.4
Koide, S.5
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18
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34247098240
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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
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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
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(2007)
J Mol Biol
, vol.368
, pp. 1024-1041
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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
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19
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33645808241
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Directed evolution to probe protein allostery and integrin I domains of 200,000-fold higher affinity
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Jin M., Song G., Carman C.V., Kim Y.-S., Astrof N.S., Shimaoka M., Wittrup D.K., and Springer T.A. Directed evolution to probe protein allostery and integrin I domains of 200,000-fold higher affinity. Proc Natl Acad Sci USA 103 (2006) 5758-5763
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(2006)
Proc Natl Acad Sci USA
, vol.103
, pp. 5758-5763
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Jin, M.1
Song, G.2
Carman, C.V.3
Kim, Y.-S.4
Astrof, N.S.5
Shimaoka, M.6
Wittrup, D.K.7
Springer, T.A.8
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20
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33745726188
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Improved mutants from directed evolution are biased to orthologous substitutions
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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
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(2006)
Protein Eng Des Sel
, vol.19
, pp. 245-253
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Cochran, J.R.1
Kim, Y.-S.2
Lippow, S.M.3
Rao, B.4
Wittrup, K.D.5
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21
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25144479800
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Characterization of T cell receptors engineered for high affinity against toxic shock syndrome toxin-1
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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
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(2005)
J Mol Biol
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Buonpane, R.A.1
Moza, B.2
Sundberg, E.J.3
Kranz, D.M.4
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22
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30044449525
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Class II-restricted T cell receptor engineered in vitro for higher affinity retains peptide specificity and function
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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.
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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.
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(2005)
Proc Natl Acad Sci USA
, vol.102
, pp. 19033-19038
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Weber, K.S.1
Donermeyer, D.L.2
Allen, P.M.3
Kranz, D.M.4
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23
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34250000045
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Neutralization of staphylococcal enterotoxin B by soluble, high-affinity receptor antagonists
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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.
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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.
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(2007)
Nat Med
, vol.13
, pp. 725-729
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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
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24
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0033536626
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Yeast polypeptide fusion surface display levels predict thermal stability and soluble secretion efficiency
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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
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(1999)
J Mol Biol
, vol.292
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Shusta, E.V.1
Kieke, M.C.2
Parke, E.3
Kranz, D.M.4
Wittrup, K.D.5
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26
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33746266938
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Directed evolution for improved secretion of cancer-testis antigen NY-ESO-1 from yeast
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Piatesi A., Howland S.W., Rakestraw J.A., Renner C., Robson N., Cebon J., Maraskovsky E., Ritter G., Old L., and Wittrup K.D. Directed evolution for improved secretion of cancer-testis antigen NY-ESO-1 from yeast. Protein Expr Purif 48 (2006) 232-242
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(2006)
Protein Expr Purif
, vol.48
, pp. 232-242
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Piatesi, A.1
Howland, S.W.2
Rakestraw, J.A.3
Renner, C.4
Robson, N.5
Cebon, J.6
Maraskovsky, E.7
Ritter, G.8
Old, L.9
Wittrup, K.D.10
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27
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33644846817
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Directed evolution of the epidermal growth factor receptor extracellular domain for expression in yeast
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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
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(2006)
Proteins Struct Funct Bioinformatics
, vol.62
, pp. 1026-1035
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Kim, Y.-S.1
Bhandari, R.2
Cochran, J.R.3
Kuriyan, J.4
Wittrup, K.D.5
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28
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33646250654
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Limitations of yeast surface display in engineering proteins of high thermostability
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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
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(2006)
Protein Eng Des Sel
, vol.19
, pp. 211-217
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Park, S.1
Xu, Y.2
Stowell, X.F.3
Gai, F.4
Saven, J.G.5
Boder, E.T.6
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29
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33847181688
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A novel high-throughput screen reveals yeast genes that increase secretion of heterologous proteins
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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
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Appl Environ Microbiol
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, pp. 1189-1198
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Wentz, A.E.1
Shusta, E.V.2
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30
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33747180836
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A flow cytometric assay for screening improved heterologous protein secretion in yeast
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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
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(2006)
Biotechnol Prog
, vol.22
, pp. 1200-1208
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Rakestraw, J.A.1
Baskaran, A.R.2
Wittrup, K.D.3
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31
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4344589735
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Fine epitope mapping of anti-epidermal growth factor receptor antibodies through random mutagenesis and yeast surface display
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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.
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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.
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(2004)
J Mol Biol
, vol.342
, pp. 539-550
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Chao, G.1
Cochran, J.R.2
Dane Wittrup, K.3
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32
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21044448356
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Development of a humanized monoclonal antibody with therapeutic potential against West Nile Virus
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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.
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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.
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(2005)
Nat Med
, vol.11
, pp. 522-530
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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
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33
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26944454471
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Structural basis of West Nile Virus neutralization by a therapeutic antibody
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Nybakken G.E., Oliphant T., Johnson S., Burke S., Diamond M.S., and Fremont D.H. Structural basis of West Nile Virus neutralization by a therapeutic antibody. Nature 437 (2005) 764-769
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(2005)
Nature
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Nybakken, G.E.1
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Johnson, S.3
Burke, S.4
Diamond, M.S.5
Fremont, D.H.6
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34
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27744601405
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Protective and therapeutic capacity of human single-chain Fv-Fc fusion proteins against West Nile Virus
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Gould L.H., Sui J., Foellmer H., Oliphant T., Wang T., Ledizet M., Murakami A., Noonan K., Lambeth C., Kar K., et al. Protective and therapeutic capacity of human single-chain Fv-Fc fusion proteins against West Nile Virus. J Virol 79 (2005) 14606-14613
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J Virol
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Gould, L.H.1
Sui, J.2
Foellmer, H.3
Oliphant, T.4
Wang, T.5
Ledizet, M.6
Murakami, A.7
Noonan, K.8
Lambeth, C.9
Kar, K.10
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35
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33845389501
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Antibody recognition and neutralization determinants on domains I and II of West Nile Virus envelope protein
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Oliphant T., Nybakken G.E., Engle M., Xu Q., Nelson C.A., Sukupolvi-Petty S., Marri A., Lachmi B.-E., Olshevsky U., Fremont D.H., et al. Antibody recognition and neutralization determinants on domains I and II of West Nile Virus envelope protein. J Virol 80 (2006) 12149-12159
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J Virol
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Oliphant, T.1
Nybakken, G.E.2
Engle, M.3
Xu, Q.4
Nelson, C.A.5
Sukupolvi-Petty, S.6
Marri, A.7
Lachmi, B.-E.8
Olshevsky, U.9
Fremont, D.H.10
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36
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31144442443
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Antibodies against West Nile Virus nonstructural protein NS1 prevent lethal infection through Fc γ receptor-dependent and -independent mechanisms
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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
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J Virol
, vol.80
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Chung, K.M.1
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