메뉴 건너뛰기




Volumn 3, Issue 1, 2009, Pages 19-27

Therapeutic antibodies and other proteins obtained by molecular display technologies

Author keywords

Affibody; Fc domain; Molecular display; Monoclonal antibody; Phage; Ribosome; Romiplostim; Therapeutic antibody; TPO; Yeast

Indexed keywords

BUDGET CONTROL; CELLS; CYTOLOGY; GENETIC ENGINEERING;

EID: 62149115313     PISSN: 18722083     EISSN: None     Source Type: Journal    
DOI: 10.2174/187220809787172641     Document Type: Review
Times cited : (9)

References (98)
  • 1
    • 0016756272 scopus 로고
    • Continuous cultures of fused cells secreting antibody of predefined specificity
    • Köhler G, Milstein C. Continuous cultures of fused cells secreting antibody of predefined specificity. Nature 1975; 256: 495-497.
    • (1975) Nature , vol.256 , pp. 495-497
    • Köhler, G.1    Milstein, C.2
  • 2
    • 0023806938 scopus 로고
    • Infections in patients receiving OKT3 monoclonal antibody for cardiac rejection: Results of a small clinical trial
    • Sinnott JT 4th, Cullison JP, Sweeney MS, Weinstein SS. Infections in patients receiving OKT3 monoclonal antibody for cardiac rejection: Results of a small clinical trial. Tex Heart Inst J 1988; 15: 102-106.
    • (1988) Tex Heart Inst J , vol.15 , pp. 102-106
    • Sinnott 4th, J.T.1    Cullison, J.P.2    Sweeney, M.S.3    Weinstein, S.S.4
  • 3
    • 0021999401 scopus 로고
    • Human anti-murine immunoglobulin responses in patients receiving monoclonal antibody therapy
    • Schroff RW, Foon KA, Beatty SM, Oldham RK, Morgan AC Jr. Human anti-murine immunoglobulin responses in patients receiving monoclonal antibody therapy. Cancer Res 1985; 45: 879-885.
    • (1985) Cancer Res , vol.45 , pp. 879-885
    • Schroff, R.W.1    Foon, K.A.2    Beatty, S.M.3    Oldham, R.K.4    Morgan Jr., A.C.5
  • 4
    • 0022355587 scopus 로고
    • Human immune response to multiple injections of murine monoclonal IgG
    • Shawler DL, Bartholomew RM, Smith LM, Dillman RO. Human immune response to multiple injections of murine monoclonal IgG. J Immunol 1985; 135: 1530-1535.
    • (1985) J Immunol , vol.135 , pp. 1530-1535
    • Shawler, D.L.1    Bartholomew, R.M.2    Smith, L.M.3    Dillman, R.O.4
  • 5
    • 0021716682 scopus 로고
    • Chimeric human antibody molecules: Mouse antigen-binding domains with human constant region domains
    • Morrison SL, Johnson MJ, Herzenberg LA, Oi VT. Chimeric human antibody molecules: Mouse antigen-binding domains with human constant region domains. Proc Natl Acad Sci USA 1984; 81: 6851-6855.
    • (1984) Proc Natl Acad Sci USA , vol.81 , pp. 6851-6855
    • Morrison, S.L.1    Johnson, M.J.2    Herzenberg, L.A.3    Oi, V.T.4
  • 6
    • 0021713342 scopus 로고
    • Production of functional chimaeric mouse/human antibody
    • Boulianne GL, Hozumi N, Shulman MJ. Production of functional chimaeric mouse/human antibody. Nature 1984; 312: 643-646.
    • (1984) Nature , vol.312 , pp. 643-646
    • Boulianne, G.L.1    Hozumi, N.2    Shulman, M.J.3
  • 7
    • 0023920595 scopus 로고
    • Reshaping human antibodies: Grafting an antilysozyme activity
    • Verhoeyen M, Milstein C, Winter G. Reshaping human antibodies: grafting an antilysozyme activity. Science 1988; 239: 1534-1536.
    • (1988) Science , vol.239 , pp. 1534-1536
    • Verhoeyen, M.1    Milstein, C.2    Winter, G.3
  • 9
    • 3242720345 scopus 로고    scopus 로고
    • Cetuximab monotherapy and cetuximab plus irinotecan in irinotecan-refractory metastatic colorectal cancer
    • Cunningham D, Humblet Y, Siena S, et al. Cetuximab monotherapy and cetuximab plus irinotecan in irinotecan-refractory metastatic colorectal cancer. N Engl J Med 2004; 351: 337-345.
    • (2004) N Engl J Med , vol.351 , pp. 337-345
    • Cunningham, D.1    Humblet, Y.2    Siena, S.3
  • 10
    • 10444267243 scopus 로고    scopus 로고
    • Cetuximab (Erbitux)-an emerging targeted therapy for epidermal growth factor receptor-expressing tumours
    • Ng M, Cunningham D. Cetuximab (Erbitux)-an emerging targeted therapy for epidermal growth factor receptor-expressing tumours. Int J Clin Pract 2004; 58: 970-976.
    • (2004) Int J Clin Pract , vol.58 , pp. 970-976
    • Ng, M.1    Cunningham, D.2
  • 11
    • 0021818675 scopus 로고
    • Filamentous fusion phage: Novel expression vectors that display cloned antigens on the virion surface
    • Smith GP. Filamentous fusion phage: Novel expression vectors that display cloned antigens on the virion surface. Science 1985; 228: 1315-1317.
    • (1985) Science , vol.228 , pp. 1315-1317
    • Smith, G.P.1
  • 12
    • 0025112794 scopus 로고
    • Searching for peptide ligands with an epitope library
    • Scott JK, Smith GP. Searching for peptide ligands with an epitope library. Science 1990; 249: 386-390.
    • (1990) Science , vol.249 , pp. 386-390
    • Scott, J.K.1    Smith, G.P.2
  • 13
    • 0025740577 scopus 로고
    • Multi-subunit proteins on the surface of filamentous phage: Methodologies for displaying antibody (Fab) heavy and light chains
    • Hoogenboom HR, Griffiths AD, Johnson KS, Chiswell DJ, Hudson P, Winter G. Multi-subunit proteins on the surface of filamentous phage: Methodologies for displaying antibody (Fab) heavy and light chains. Nucleic Acids Res 1991; 19: 4133-4137.
    • (1991) Nucleic Acids Res , vol.19 , pp. 4133-4137
    • Hoogenboom, H.R.1    Griffiths, A.D.2    Johnson, K.S.3    Chiswell, D.J.4    Hudson, P.5    Winter, G.6
  • 14
    • 0031945007 scopus 로고    scopus 로고
    • Evolving catalytic antibodies in a phage-displayed combinatorial library
    • Fujii I, Fukuyama S, Iwabuchi Y, Tanimura R. Evolving catalytic antibodies in a phage-displayed combinatorial library. Nat Biotechnol 1998; 16: 463-467.
    • (1998) Nat Biotechnol , vol.16 , pp. 463-467
    • Fujii, I.1    Fukuyama, S.2    Iwabuchi, Y.3    Tanimura, R.4
  • 16
    • 0028942281 scopus 로고
    • Surface expression and ligand-based selection of cDNAs fused to filamentous phage gene VI
    • Jespers LS, Messens JH, De Keyser A, et al. Surface expression and ligand-based selection of cDNAs fused to filamentous phage gene VI. Biotechnology (NY) 1995; 13: 378-382.
    • (1995) Biotechnology (NY) , vol.13 , pp. 378-382
    • Jespers, L.S.1    Messens, J.H.2    De Keyser, A.3
  • 17
    • 0035471140 scopus 로고    scopus 로고
    • Protein design and phage display
    • Hoess RH. Protein design and phage display. Chem Rev 2001; 101: 3205-3218.
    • (2001) Chem Rev , vol.101 , pp. 3205-3218
    • Hoess, R.H.1
  • 18
    • 0033022120 scopus 로고    scopus 로고
    • Making artificial antibodies: A format for phage display of combinatorial heterodimeric arrays
    • Gao C, Mao S, Lo CH, Wirsching P, Lerner RA, Janda KD. Making artificial antibodies: A format for phage display of combinatorial heterodimeric arrays. Proc Natl Acad Sci USA 1999; 96: 6025-6030.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 6025-6030
    • Gao, C.1    Mao, S.2    Lo, C.H.3    Wirsching, P.4    Lerner, R.A.5    Janda, K.D.6
  • 19
    • 0029008514 scopus 로고
    • Glutathione transferases with novel active sites isolated by phage display from a library of random mutants
    • Widersten M, Mannervik B. Glutathione transferases with novel active sites isolated by phage display from a library of random mutants. J Mol Biol 1995; 250: 115-122.
    • (1995) J Mol Biol , vol.250 , pp. 115-122
    • Widersten, M.1    Mannervik, B.2
  • 20
    • 0030955262 scopus 로고    scopus 로고
    • Mechanism-based phage display selection of active-site mutants of human glutathione transferase A1-1 catalyzing SNAr reactions
    • Hansson LO, Widersten M, Mannervik B. Mechanism-based phage display selection of active-site mutants of human glutathione transferase A1-1 catalyzing SNAr reactions. Biochemistry 1997; 36: 11252-11260.
    • (1997) Biochemistry , vol.36 , pp. 11252-11260
    • Hansson, L.O.1    Widersten, M.2    Mannervik, B.3
  • 23
    • 0030924508 scopus 로고    scopus 로고
    • Phage display of a catalytic antibody to optimize affinity for transition-state analog binding
    • Baca M, Scanlan TS, Stephenson RC, Wells JA. Phage display of a catalytic antibody to optimize affinity for transition-state analog binding. Proc Natl Acad Sci USA 1997; 94: 10063-10068.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 10063-10068
    • Baca, M.1    Scanlan, T.S.2    Stephenson, R.C.3    Wells, J.A.4
  • 29
    • 0002013346 scopus 로고    scopus 로고
    • Filamentous phage biology
    • Barbas CF, Burton DR, Scott JK, Silverman, Eds, Cold Spring Harbor Laboratory Press, Cold Spring Harbor
    • Webster R. Filamentous phage biology. In: Barbas CF, Burton DR, Scott JK, Silverman, Eds. Phage Display: A laboratory manual. Cold Spring Harbor Laboratory Press, Cold Spring Harbor 2001.
    • (2001) Phage Display: A laboratory manual
    • Webster, R.1
  • 30
    • 85187880672 scopus 로고    scopus 로고
    • Watkins, B.A., Reitz, M.S.J.: WO01000678 (2001).
    • Watkins, B.A., Reitz, M.S.J.: WO01000678 (2001).
  • 31
    • 85187883635 scopus 로고    scopus 로고
    • Furuichi, Y., Komiyama, T.: WO2006093071 (2006).
    • Furuichi, Y., Komiyama, T.: WO2006093071 (2006).
  • 32
    • 85187872105 scopus 로고    scopus 로고
    • Andersen, P.S., Buus, S., Engberg, J., Fugger, L., Stryhn, A.: WO97002342 (1997).
    • Andersen, P.S., Buus, S., Engberg, J., Fugger, L., Stryhn, A.: WO97002342 (1997).
  • 33
    • 14744300636 scopus 로고
    • Specific adhesion and hydrolysis of cellulose by intact Escherichia coli expressing surface anchored cellulase or cellulose binding domains
    • Francisco JA, Stathopoulos C, Warren RA, Kilburn DG, Georgiou G. Specific adhesion and hydrolysis of cellulose by intact Escherichia coli expressing surface anchored cellulase or cellulose binding domains. Biotechnology (NY) 1993; 11: 491-495.
    • (1993) Biotechnology (NY) , vol.11 , pp. 491-495
    • Francisco, J.A.1    Stathopoulos, C.2    Warren, R.A.3    Kilburn, D.G.4    Georgiou, G.5
  • 34
    • 0035212525 scopus 로고    scopus 로고
    • Display of passenger proteins on the surface of Escherichia coli K-12 by the enterohemorrhagic E. coli intimin EaeA
    • Wentzel A, Christmann A, Adams T, Kolmar H. Display of passenger proteins on the surface of Escherichia coli K-12 by the enterohemorrhagic E. coli intimin EaeA. J Bacteriol 2001; 183: 7273-7284.
    • (2001) J Bacteriol , vol.183 , pp. 7273-7284
    • Wentzel, A.1    Christmann, A.2    Adams, T.3    Kolmar, H.4
  • 35
    • 0024815641 scopus 로고
    • Type 1 fimbriae of Escherichia coli as carriers of heterologous antigenic sequences
    • Hedegaard L, Klemm P. Type 1 fimbriae of Escherichia coli as carriers of heterologous antigenic sequences. Gene 1989; 85: 115-124.
    • (1989) Gene , vol.85 , pp. 115-124
    • Hedegaard, L.1    Klemm, P.2
  • 36
    • 0033861792 scopus 로고    scopus 로고
    • Peptide display on bacterial flagella: Principles and applications
    • Westerlund-Wikström B. Peptide display on bacterial flagella: Principles and applications. Int J Med Microbiol 2000; 290: 223-230.
    • (2000) Int J Med Microbiol , vol.290 , pp. 223-230
    • Westerlund-Wikström, B.1
  • 37
    • 0032818328 scopus 로고    scopus 로고
    • Engineering of a Staphylococcus carnosus surface display system by substitution or deletion of a Staphylococcus hyicus lipase propeptide
    • Samuelson P, Cano F, Robert A, Sth̊l S. Engineering of a Staphylococcus carnosus surface display system by substitution or deletion of a Staphylococcus hyicus lipase propeptide. FEMS Microbiol Lett 1999; 179: 131-139.
    • (1999) FEMS Microbiol Lett , vol.179 , pp. 131-139
    • Samuelson, P.1    Cano, F.2    Robert, A.3    Sth̊l, S.4
  • 38
    • 33644859125 scopus 로고    scopus 로고
    • Display of alpha-amylase on the surface of Lactobacillus casei cells by use of the PgsA anchor protein, and production of lactic acid from starch
    • Narita J, Okano K, Kitao T, et al. Display of alpha-amylase on the surface of Lactobacillus casei cells by use of the PgsA anchor protein, and production of lactic acid from starch. Appl Environ Microbiol 2006; 72: 269-275.
    • (2006) Appl Environ Microbiol , vol.72 , pp. 269-275
    • Narita, J.1    Okano, K.2    Kitao, T.3
  • 39
    • 0030956641 scopus 로고    scopus 로고
    • Cell wall anchoring of the Streptococcus pyogenes M6 protein in various lactic acid bacteria
    • Piard JC, Hautefort I, Fischetti VA, Ehrlich SD, Fons M, Gruss A. Cell wall anchoring of the Streptococcus pyogenes M6 protein in various lactic acid bacteria. J Bacteriol 1997; 179: 3068-3072.
    • (1997) J Bacteriol , vol.179 , pp. 3068-3072
    • Piard, J.C.1    Hautefort, I.2    Fischetti, V.A.3    Ehrlich, S.D.4    Fons, M.5    Gruss, A.6
  • 40
    • 0036268822 scopus 로고    scopus 로고
    • Lactobacillus bulgaricus proteinase expressed in Lactococcu lactis is a powerful carrier for cell wall-associated and secreted bovine beta-lactoglobulin fusion proteins
    • Bernasconi E, Germond JE, Delley M, Fritsché R, Corthésy B. Lactobacillus bulgaricus proteinase expressed in Lactococcu lactis is a powerful carrier for cell wall-associated and secreted bovine beta-lactoglobulin fusion proteins. Appl Environ Microbiol 2002; 68: 2917-2923.
    • (2002) Appl Environ Microbiol , vol.68 , pp. 2917-2923
    • Bernasconi, E.1    Germond, J.E.2    Delley, M.3    Fritsché, R.4    Corthésy, B.5
  • 41
    • 0034045526 scopus 로고    scopus 로고
    • Genetic immobilization of proteins on the yeast cell surface
    • Ueda M, Tanaka A. Genetic immobilization of proteins on the yeast cell surface. Biotechnol Adv 2000; 18: 121-140.
    • (2000) Biotechnol Adv , vol.18 , pp. 121-140
    • Ueda, M.1    Tanaka, A.2
  • 42
    • 0033803961 scopus 로고    scopus 로고
    • Cell surface engineering of yeast: Construction of arming yeast with biocatalyst
    • Ueda M, Tanaka A. Cell surface engineering of yeast: Construction of arming yeast with biocatalyst. J Biosci Bioeng 2000; 90: 125-136.
    • (2000) J Biosci Bioeng , vol.90 , pp. 125-136
    • Ueda, M.1    Tanaka, A.2
  • 43
    • 1642340053 scopus 로고    scopus 로고
    • Yeast cell-surface display-applications of molecular display
    • Kondo A, Ueda M. Yeast cell-surface display-applications of molecular display. Appl Microbiol Biotechnol 2004; 64: 28-40.
    • (2004) Appl Microbiol Biotechnol , vol.64 , pp. 28-40
    • Kondo, A.1    Ueda, M.2
  • 44
    • 85187899650 scopus 로고    scopus 로고
    • Fukuda, H., Kondo, A., Tanaka, A., Ueda, M., Satoh, E.: WO03016525 ( 2003).
    • Fukuda, H., Kondo, A., Tanaka, A., Ueda, M., Satoh, E.: WO03016525 ( 2003).
  • 45
    • 85187883744 scopus 로고    scopus 로고
    • Kondo, A., Kuroda, S., Ueda, M., Fukuda, H., Tatematsu, K., Yamazaki, T.: WO2006104254 (2006).
    • Kondo, A., Kuroda, S., Ueda, M., Fukuda, H., Tatematsu, K., Yamazaki, T.: WO2006104254 (2006).
  • 46
    • 0003179107 scopus 로고    scopus 로고
    • Arming yeast with cell-surface catalysts
    • 75:, Anonymous
    • Anonymous. Arming yeast with cell-surface catalysts. Chem Eng News 1997; 75: 32.
    • (1997) Chem Eng News , pp. 32
  • 47
    • 85187878011 scopus 로고    scopus 로고
    • Shibasaki S, Maeda H, Ueda M. Molecular display technology using yeast - Arming technology. Anal Sci 2009; 1: (in press).
    • Shibasaki S, Maeda H, Ueda M. Molecular display technology using yeast - Arming technology. Anal Sci 2009; 1: (in press).
  • 48
    • 85187899543 scopus 로고    scopus 로고
    • Mattheakis LC, Bhatt RR, Dower WJ. An in vitro polysome display system for identifying ligands from very large peptide libraries. Proc Natl Acad Sci USA 1994; 91: 9022-9026.
    • Mattheakis LC, Bhatt RR, Dower WJ. An in vitro polysome display system for identifying ligands from very large peptide libraries. Proc Natl Acad Sci USA 1994; 91: 9022-9026.
  • 49
    • 0030974119 scopus 로고    scopus 로고
    • In vitro selection and evolution of functional proteins by using ribosome display
    • Hanes J, Plückthun A. In vitro selection and evolution of functional proteins by using ribosome display. Proc Natl Acad Sci USA 1997; 94: 4937-4942.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 4937-4942
    • Hanes, J.1    Plückthun, A.2
  • 50
    • 85187909020 scopus 로고    scopus 로고
    • US5643768
    • Kawasaki, G.H.: US5643768 (1997).
    • (1997)
    • Kawasaki, G.H.1
  • 52
    • 85187875023 scopus 로고    scopus 로고
    • Buchanan, A., Jermutus, L., Walton, S.: WO2006072773 (2006).
    • Buchanan, A., Jermutus, L., Walton, S.: WO2006072773 (2006).
  • 53
    • 38649127253 scopus 로고    scopus 로고
    • New drugs for familiar therapeutic targets: Thrombopoietin receptor agonists and immune thrombocytopenic purpura
    • Kuter DJ. New drugs for familiar therapeutic targets: Thrombopoietin receptor agonists and immune thrombocytopenic purpura. Eur J Haematol Suppl 2008; 69: 9-18.
    • (2008) Eur J Haematol Suppl , vol.69 , pp. 9-18
    • Kuter, D.J.1
  • 54
    • 33749249751 scopus 로고    scopus 로고
    • A rationally designed agonist antibody fragment that functionally mimics thrombopoietin
    • Frederickson S, Renshaw MW, Lin B, et al. A rationally designed agonist antibody fragment that functionally mimics thrombopoietin. Proc Natl Acad Sci USA 2006; 103:14307-14312.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 14307-14312
    • Frederickson, S.1    Renshaw, M.W.2    Lin, B.3
  • 55
    • 0037111558 scopus 로고    scopus 로고
    • Recombinant human thrombopoietin: Basic biology and evaluation of clinical studies
    • Kuter DJ, Begley CG. Recombinant human thrombopoietin: basic biology and evaluation of clinical studies. Blood 2002; 100: 3457-3469.
    • (2002) Blood , vol.100 , pp. 3457-3469
    • Kuter, D.J.1    Begley, C.G.2
  • 57
    • 0034656323 scopus 로고    scopus 로고
    • Effects of megakaryocyte growth and development factor on platelet production, platelet life span, and platelet function in healthy human volunteers
    • Harker LA, Roskos LK, Marzec UM, et al. Effects of megakaryocyte growth and development factor on platelet production, platelet life span, and platelet function in healthy human volunteers. Blood 2000; 95: 2514-2522.
    • (2000) Blood , vol.95 , pp. 2514-2522
    • Harker, L.A.1    Roskos, L.K.2    Marzec, U.M.3
  • 58
    • 0030966361 scopus 로고    scopus 로고
    • Stimulation of megakaryocyte and platelet production by a single dose of recombinant human thrombopoietin in patients with cancer
    • Vadhan-Raj S, Murray LJ, Bueso-Ramos C, et al. Stimulation of megakaryocyte and platelet production by a single dose of recombinant human thrombopoietin in patients with cancer. Ann Intern Med 1997; 126: 673-681.
    • (1997) Ann Intern Med , vol.126 , pp. 673-681
    • Vadhan-Raj, S.1    Murray, L.J.2    Bueso-Ramos, C.3
  • 59
    • 0034050651 scopus 로고    scopus 로고
    • Recombinant human thrombopoietin attenuates carboplatininduced severe thrombocytopenia and the need for platelet transfusions in patients with gynecologic cancer
    • Vadhan-Raj S, Verschraegen CF, Bueso-Ramos C, et al. Recombinant human thrombopoietin attenuates carboplatininduced severe thrombocytopenia and the need for platelet transfusions in patients with gynecologic cancer. Ann Intern Med 2000; 132: 364-368.
    • (2000) Ann Intern Med , vol.132 , pp. 364-368
    • Vadhan-Raj, S.1    Verschraegen, C.F.2    Bueso-Ramos, C.3
  • 60
    • 85187885489 scopus 로고    scopus 로고
    • Bartley, T.D., Bogenberger, J.M., Bosselman, R.A., Hunt, P., Kinstler, O.B., Samal, B.B.: WO95026746 (1995).
    • Bartley, T.D., Bogenberger, J.M., Bosselman, R.A., Hunt, P., Kinstler, O.B., Samal, B.B.: WO95026746 (1995).
  • 61
    • 0030773876 scopus 로고    scopus 로고
    • Peptide agonist of the thrombopoietin receptor as potent as the natural cytokine
    • Cwirla SE, Balasubramanian P, Duffin DJ, et al. Peptide agonist of the thrombopoietin receptor as potent as the natural cytokine. Science 1997; 276: 1696-1699.
    • (1997) Science , vol.276 , pp. 1696-1699
    • Cwirla, S.E.1    Balasubramanian, P.2    Duffin, D.J.3
  • 62
    • 38649120593 scopus 로고    scopus 로고
    • Efficacy of romiplostim in patients with chronic immune thrombocytopenic purpura: A double-blind randomised controlled trial
    • Kuter DJ, Bussel JB, Lyons RM, et al. Efficacy of romiplostim in patients with chronic immune thrombocytopenic purpura: a double-blind randomised controlled trial. Lancet 2008; 371: 395-403
    • (2008) Lancet , vol.371 , pp. 395-403
    • Kuter, D.J.1    Bussel, J.B.2    Lyons, R.M.3
  • 63
    • 85187903636 scopus 로고    scopus 로고
    • US20077189827
    • Feige, U.: US20077189827 (2007).
    • (2007)
    • Feige, U.1
  • 64
    • 43549101411 scopus 로고    scopus 로고
    • Alternative binding proteins: Affibody binding proteins developed from a small three-helix bundle scaffold
    • Nygren PA. Alternative binding proteins: affibody binding proteins developed from a small three-helix bundle scaffold. FEBS J 2008; 275: 2668-2676.
    • (2008) FEBS J , vol.275 , pp. 2668-2676
    • Nygren, P.A.1
  • 65
    • 27144511241 scopus 로고    scopus 로고
    • Engineering novel binding proteins from nonimmunoglobulin domains
    • Binz HK, Amstutz P, Plückthun A. Engineering novel binding proteins from nonimmunoglobulin domains. Nat Biotechnol 2005; 23: 1257-1268.
    • (2005) Nat Biotechnol , vol.23 , pp. 1257-1268
    • Binz, H.K.1    Amstutz, P.2    Plückthun, A.3
  • 67
    • 85187882280 scopus 로고    scopus 로고
    • Nilsson, B., Nygren, P.A. Uhlen, M.: WO95019374 (1995).
    • Nilsson, B., Nygren, P.A. Uhlen, M.: WO95019374 (1995).
  • 68
    • 85187911519 scopus 로고    scopus 로고
    • Ljungqvist, C., Nord, K., Nygren, P.A., Uhlen, M.: WO00063243 (2000).
    • Ljungqvist, C., Nord, K., Nygren, P.A., Uhlen, M.: WO00063243 (2000).
  • 69
    • 0028982245 scopus 로고
    • A combinatorial library of an alpha-helical bacterial receptor domain
    • Nord K, Nilsson J, Nilsson B, Uhlén M, Nygren PA. A combinatorial library of an alpha-helical bacterial receptor domain. Protein Eng 1995; 8: 601-608.
    • (1995) Protein Eng , vol.8 , pp. 601-608
    • Nord, K.1    Nilsson, J.2    Nilsson, B.3    Uhlén, M.4    Nygren, P.A.5
  • 70
    • 0030835822 scopus 로고    scopus 로고
    • Binding proteins selected from combinatorial libraries of an alpha-helical bacterial receptor domain
    • Nord K, Gunneriusson E, Ringdahl J, Ståhl S, Uhlén M, Nygren PA. Binding proteins selected from combinatorial libraries of an alpha-helical bacterial receptor domain. Nat Biotechnol 1997; 15: 772-777.
    • (1997) Nat Biotechnol , vol.15 , pp. 772-777
    • Nord, K.1    Gunneriusson, E.2    Ringdahl, J.3    Ståhl, S.4    Uhlén, M.5    Nygren, P.A.6
  • 71
    • 0034625656 scopus 로고    scopus 로고
    • Ligands selected from combinatorial libraries of protein A for use in affinity capture of apolipoprotein A-1M and taq DNA polymerase
    • Nord K, Gunneriusson E, Uhlén M, Nygren PA. Ligands selected from combinatorial libraries of protein A for use in affinity capture of apolipoprotein A-1M and taq DNA polymerase. J Biotechnol 2000; 80(1): 45-54.
    • (2000) J Biotechnol , vol.80 , Issue.1 , pp. 45-54
    • Nord, K.1    Gunneriusson, E.2    Uhlén, M.3    Nygren, P.A.4
  • 72
    • 0034832744 scopus 로고    scopus 로고
    • Recombinant human factor VIII-specific affinity ligands selected from phage-displayed combinatorial libraries of protein A
    • Nord K, Nord O, Uhlén M, Kelley B, Ljungqvist C, Nygren PA. Recombinant human factor VIII-specific affinity ligands selected from phage-displayed combinatorial libraries of protein A. Eur J Biochem 2001; 268: 4269-4277.
    • (2001) Eur J Biochem , vol.268 , pp. 4269-4277
    • Nord, K.1    Nord, O.2    Uhlén, M.3    Kelley, B.4    Ljungqvist, C.5    Nygren, P.A.6
  • 73
    • 0035423772 scopus 로고    scopus 로고
    • Dual labeling of a binding protein allows for specific fluorescence detection of native protein
    • Karlström A, Nygren PA. Dual labeling of a binding protein allows for specific fluorescence detection of native protein. Anal Biochem 2001; 295: 22-30.
    • (2001) Anal Biochem , vol.295 , pp. 22-30
    • Karlström, A.1    Nygren, P.A.2
  • 74
    • 0036498811 scopus 로고    scopus 로고
    • Construction and characterization of affibody-Fc chimeras produced in Escherichia coli
    • Rönnmark J, Hansson M, Nguyen T, et al. Construction and characterization of affibody-Fc chimeras produced in Escherichia coli. J Immunol Methods 2002; 261: 199-211.
    • (2002) J Immunol Methods , vol.261 , pp. 199-211
    • Rönnmark, J.1    Hansson, M.2    Nguyen, T.3
  • 75
    • 0142184270 scopus 로고    scopus 로고
    • Inhibition of the CD28-CD80 co-stimulation signal by a CD28-binding affibody ligand developed by combinatorial protein engineering
    • Sandström K, Xu Z, Forsberg G, Nygren PA. Inhibition of the CD28-CD80 co-stimulation signal by a CD28-binding affibody ligand developed by combinatorial protein engineering. Protein Eng 2003; 16: 691-697.
    • (2003) Protein Eng , vol.16 , pp. 691-697
    • Sandström, K.1    Xu, Z.2    Forsberg, G.3    Nygren, P.A.4
  • 76
    • 0024337144 scopus 로고
    • Studies of the HER-2/neu proto-oncogene in human breast and ovarian cancer
    • Slamon DJ, Godolphin W, Jones LA, et al. Studies of the HER-2/neu proto-oncogene in human breast and ovarian cancer. Science 1989; 244: 707-712.
    • (1989) Science , vol.244 , pp. 707-712
    • Slamon, D.J.1    Godolphin, W.2    Jones, L.A.3
  • 77
    • 0028670125 scopus 로고
    • The biology of erbB-2/neu/HER-2 and its role in cancer
    • Hynes NE, Stern DF. The biology of erbB-2/neu/HER-2 and its role in cancer. Biochim Biophys Acta 1994; 1198: 165-184.
    • (1994) Biochim Biophys Acta , vol.1198 , pp. 165-184
    • Hynes, N.E.1    Stern, D.F.2
  • 79
    • 85187892201 scopus 로고    scopus 로고
    • Lee, W.M., Walton, S.M.: WO01015730 (2001).
    • Lee, W.M., Walton, S.M.: WO01015730 (2001).
  • 80
    • 34249672864 scopus 로고    scopus 로고
    • Traastuzumab: Triumphs and tribulations
    • Nahta R, Esteva FJ. Traastuzumab: Triumphs and tribulations. Oncogene 2007; 26: 3637-3643
    • (2007) Oncogene , vol.26 , pp. 3637-3643
    • Nahta, R.1    Esteva, F.J.2
  • 81
    • 4644247278 scopus 로고    scopus 로고
    • Selection and characterization of HER2/neu-binding affibody ligands
    • Wikman M, Steffen AC, Gunneriusson E, et al. Selection and characterization of HER2/neu-binding affibody ligands. Protein Eng Des Sel 2004; 17: 455-462.
    • (2004) Protein Eng Des Sel , vol.17 , pp. 455-462
    • Wikman, M.1    Steffen, A.C.2    Gunneriusson, E.3
  • 82
    • 85187868283 scopus 로고    scopus 로고
    • Carlsson, J., Ståhl, S., Eriksson, T., Gunneriusson, E., Nilsson, F.: WO2005003156 (2005).
    • Carlsson, J., Ståhl, S., Eriksson, T., Gunneriusson, E., Nilsson, F.: WO2005003156 (2005).
  • 83
    • 33646261864 scopus 로고    scopus 로고
    • Tumor imaging using a picomolar affinity HER2 binding affibody molecule
    • Orlova A, Magnusson M, Eriksson TL, et al. Tumor imaging using a picomolar affinity HER2 binding affibody molecule. Cancer Res 2006; 66: 4339-4348.
    • (2006) Cancer Res , vol.66 , pp. 4339-4348
    • Orlova, A.1    Magnusson, M.2    Eriksson, T.L.3
  • 85
    • 0034760935 scopus 로고    scopus 로고
    • Development of novel whole-cell immunoadsorbents by yeast surface display of the IgG-binding domain
    • Nakamura Y, Shibasaki S, Ueda M, Tanaka A, Fukuda H, Kondo A. Development of novel whole-cell immunoadsorbents by yeast surface display of the IgG-binding domain. Appl Microbiol Biotechnol 2001; 57: 500-505.
    • (2001) Appl Microbiol Biotechnol , vol.57 , pp. 500-505
    • Nakamura, Y.1    Shibasaki, S.2    Ueda, M.3    Tanaka, A.4    Fukuda, H.5    Kondo, A.6
  • 86
    • 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, et al. Construction of a novel synergistic system for production and recovery of secreted recombinant proteins by the cell surface engineering. Appl Microbiol Biotechnol 2007; 75: 821-828.
    • (2007) Appl Microbiol Biotechnol , vol.75 , pp. 821-828
    • Shibasaki, S.1    Kawabata, A.2    Ishii, J.3
  • 87
    • 34547574021 scopus 로고    scopus 로고
    • High-efficiency recovery of target cells using improved yeast display system for detection of protein-protein interactions
    • Fukuda N, Ishii J, Shibasaki S, Ueda M, Fukuda H, Kondo A. High-efficiency recovery of target cells using improved yeast display system for detection of protein-protein interactions. Appl Microbiol Biotechnol 2007; 76: 151-158.
    • (2007) Appl Microbiol Biotechnol , vol.76 , pp. 151-158
    • Fukuda, N.1    Ishii, J.2    Shibasaki, S.3    Ueda, M.4    Fukuda, H.5    Kondo, A.6
  • 89
    • 2442535239 scopus 로고    scopus 로고
    • Comparison of two forms of catalytic antibody displayed on yeast-cell surface
    • Lin Y, Shiraga S, Tsumuraya T, et al. Comparison of two forms of catalytic antibody displayed on yeast-cell surface. J Mol Catl B Enzym 2004; 28: 241-246.
    • (2004) J Mol Catl B Enzym , vol.28 , pp. 241-246
    • Lin, Y.1    Shiraga, S.2    Tsumuraya, T.3
  • 90
    • 2442484962 scopus 로고    scopus 로고
    • Isolation of novel catalytic antibody clones from combinatorial library displayed on yeast-cell surface
    • Lin Y, Shiraga S, Tsumuraya T, et al. Isolation of novel catalytic antibody clones from combinatorial library displayed on yeast-cell surface. J Mol Catl B Enzym 2004; 28: 247-251.
    • (2004) J Mol Catl B Enzym , vol.28 , pp. 247-251
    • Lin, Y.1    Shiraga, S.2    Tsumuraya, T.3
  • 91
    • 46149105175 scopus 로고    scopus 로고
    • Construction of cell surface-engineered yeasts displaying antigen to detect antibodies by immunofluorescence and yeast-ELISA
    • Tang YQ, Ueda M, Lin Y, et al. Construction of cell surface-engineered yeasts displaying antigen to detect antibodies by immunofluorescence and yeast-ELISA. Appl Microbiol Biotechnol 2008; 79: 1019-1026.
    • (2008) Appl Microbiol Biotechnol , vol.79 , pp. 1019-1026
    • Tang, Y.Q.1    Ueda, M.2    Lin, Y.3
  • 93
    • 35148855712 scopus 로고    scopus 로고
    • Computational design of antibody-affinity improvement beyond in vivo maturation
    • Lippow SM, Wittrup KD, Tidor B. Computational design of antibody-affinity improvement beyond in vivo maturation. Nat Biotechnol 2007; 25: 1171-1176.
    • (2007) Nat Biotechnol , vol.25 , pp. 1171-1176
    • Lippow, S.M.1    Wittrup, K.D.2    Tidor, B.3
  • 94
    • 38949155234 scopus 로고    scopus 로고
    • Fluorogen-activating single-chain antibodies for imaging cell surface proteins
    • Szent-Gyorgyi C, Schmidt BF, Creeger Y, et al. Fluorogen-activating single-chain antibodies for imaging cell surface proteins. Nat Biotechnol 2008; 26: 235-240.
    • (2008) Nat Biotechnol , vol.26 , pp. 235-240
    • Szent-Gyorgyi, C.1    Schmidt, B.F.2    Creeger, Y.3
  • 95
    • 85187865318 scopus 로고    scopus 로고
    • Siegel, R.W., Tyner, J.D., Nakagawa, T.Y.: WO2008054517 (2008).
    • Siegel, R.W., Tyner, J.D., Nakagawa, T.Y.: WO2008054517 (2008).
  • 96
    • 85187910678 scopus 로고    scopus 로고
    • Shusta, E.V., Wang, X.X., Cho, Y.P.: WO2007143711(2007).
    • Shusta, E.V., Wang, X.X., Cho, Y.P.: WO2007143711(2007).
  • 97
    • 33747152520 scopus 로고    scopus 로고
    • Construction of a cultivation system of a yeast single cell in a cell chip microchamber
    • Fukuda T, Shiraga S, Kato M, Suye S, Ueda M. Construction of a cultivation system of a yeast single cell in a cell chip microchamber. Biotechnol Prog 2006; 22: 944-948.
    • (2006) Biotechnol Prog , vol.22 , pp. 944-948
    • Fukuda, T.1    Shiraga, S.2    Kato, M.3    Suye, S.4    Ueda, M.5
  • 98
    • 2442554182 scopus 로고    scopus 로고
    • Combinatorial bioengineering-Development of molecular evolution
    • Ueda M, Kondo A. Combinatorial bioengineering-Development of molecular evolution. J Mol Catl B Enzym 2004; 28: 137.
    • (2004) J Mol Catl B Enzym , vol.28 , pp. 137
    • Ueda, M.1    Kondo, A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.