메뉴 건너뛰기




Volumn , Issue , 2010, Pages 1-79

Phage display as a tool for synthetic biology

Author keywords

[No Author keywords available]

Indexed keywords


EID: 84896239067     PISSN: None     EISSN: None     Source Type: Book    
DOI: None     Document Type: Book
Times cited : (4)

References (290)
  • 1
    • 0028962883 scopus 로고
    • Characterization of phage that bind plastic from phage-displayed random peptide libraries
    • Adey, N. B., Mataragnon, A. H., Rider, J. E., Carter, J. M., & Kay, B. K. (1995). Characterization of phage that bind plastic from phage-displayed random peptide libraries. Gene, 156, 27-31.
    • (1995) Gene , vol.156 , pp. 27-31
    • Adey, N.B.1    Mataragnon, A.H.2    Rider, J.E.3    Carter, J.M.4    Kay, B.K.5
  • 2
    • 84892125662 scopus 로고    scopus 로고
    • Recent Advances in microbial discovery using metagenomics, DNA microarray, biosensors, molecular subtyping, and phage recombinant probes
    • In M. K. Moretti & L. J. Rizzo (Eds.), Chapter 4, Nova Science Publishers, Inc
    • Al-Khaldi, S. F., Mossoba, M. M., Yakes, B. J., Brown, E., Sharma, D., & Carnazza, S. (2008). Recent Advances in microbial discovery using metagenomics, DNA microarray, biosensors, molecular subtyping, and phage recombinant probes. In M. K. Moretti & L. J. Rizzo (Eds.), Oligonucleotide Array Sequence Analysis (Chapter 4, pp. 123-147). Nova Science Publishers, Inc.
    • (2008) Oligonucleotide Array Sequence Analysis , pp. 123-147
    • Al-Khaldi, S.F.1    Mossoba, M.M.2    Yakes, B.J.3    Brown, E.4    Sharma, D.5    Carnazza, S.6
  • 3
    • 84892018144 scopus 로고    scopus 로고
    • The biggest winners in DNA and protein sequence analysis: metagenomics, DNA microarray, biosensors, molecular subtyping, and phage recombinant probes
    • Nova Science Publishers
    • Al-Khaldi, S. F., Mossoba, M. M., Yakes, B. J., Brown, E., Sharma, D., & Carnazza, S. (2009). The biggest winners in DNA and protein sequence analysis: metagenomics, DNA microarray, biosensors, molecular subtyping, and phage recombinant probes. International Journal of Medical and Biological Frontiers (Nova Science Publishers), 15(3/4), 4.
    • (2009) International Journal of Medical and Biological Frontiers , vol.15 , Issue.3-4 , pp. 4
    • Al-Khaldi, S.F.1    Mossoba, M.M.2    Yakes, B.J.3    Brown, E.4    Sharma, D.5    Carnazza, S.6
  • 5
    • 0035424963 scopus 로고    scopus 로고
    • In vitro display technologies: novel developments and applications
    • Amstutz, P., Forrer, P., Zahnd, C., & Plückthun, A. (2001). In vitro display technologies: novel developments and applications. Curr. Opin. Biotechnol., 12, 400-5.
    • (2001) Curr. Opin. Biotechnol. , vol.12 , pp. 400-405
    • Amstutz, P.1    Forrer, P.2    Zahnd, C.3    Plückthun, A.4
  • 7
    • 0001270261 scopus 로고    scopus 로고
    • Design by directed evolution
    • Arnold, F. H. (1998). Design by directed evolution. Acc. Chem. Res., 31(3), 125-31.
    • (1998) Acc. Chem. Res. , vol.31 , Issue.3 , pp. 125-131
    • Arnold, F.H.1
  • 9
    • 0027449373 scopus 로고
    • Identification of a hexapeptide that mimics a conformation-dependent binding site of acetylcholine receptor by use of a phage-epitope library
    • Balass, M., Heldman, Y., Cabilly, S., Givol, D., Katchalski-Katzir, E., & Fuchs, S. (1993). Identification of a hexapeptide that mimics a conformation-dependent binding site of acetylcholine receptor by use of a phage-epitope library. Proc. Natl. Acad. Sci. USA, 90, 10638-42.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 10638-10642
    • Balass, M.1    Heldman, Y.2    Cabilly, S.3    Givol, D.4    Katchalski-Katzir, E.5    Fuchs, S.6
  • 10
    • 33845455825 scopus 로고    scopus 로고
    • Lytic phage as a specific and selective probe for detection of Staphylococcus aureus. A surface plasmon resonance spectroscopic study
    • Balasubramanian, S., Sorokulova, I. B., Vodyanoy, V. J., & Simonian, A. L. (2007). Lytic phage as a specific and selective probe for detection of Staphylococcus aureus. A surface plasmon resonance spectroscopic study. Biosens. Bioelectr., 22, 948-55.
    • (2007) Biosens. Bioelectr. , vol.22 , pp. 948-955
    • Balasubramanian, S.1    Sorokulova, I.B.2    Vodyanoy, V.J.3    Simonian, A.L.4
  • 11
    • 12344295408 scopus 로고    scopus 로고
    • Synthetic biology for nanotechnology. Tutorial
    • Ball, P. (2005). Synthetic biology for nanotechnology. Tutorial. Nanotechnology, 16, R1-R8.
    • (2005) Nanotechnology , vol.16
    • Ball, P.1
  • 12
    • 0026563253 scopus 로고
    • Semisynthetic combinatorial libraries: a chemical solution to the diversity problem
    • Barbas, C. F., Bain, J. D., Hoekstra, D. M., & Lerner, R. A. (1992). Semisynthetic combinatorial libraries: a chemical solution to the diversity problem. Proc. Natl. Acad. Sci. USA, 89, 4457-61.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 4457-4461
    • Barbas, C.F.1    Bain, J.D.2    Hoekstra, D.M.3    Lerner, R.A.4
  • 13
    • 0025838021 scopus 로고
    • Assembly of combinatorial antibody libraries on phage surfaces: the gene III site
    • Barbas, C. F., Kang, A. S., Lerner, R. A., & Benkovic, S. J. (1991). Assembly of combinatorial antibody libraries on phage surfaces: the gene III site. Proc. Natl. Acad. Sci. USA, 88, 7978-82.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 7978-7982
    • Barbas, C.F.1    Kang, A.S.2    Lerner, R.A.3    Benkovic, S.J.4
  • 14
    • 0036839270 scopus 로고    scopus 로고
    • Sequence analysis of an artificial family of RNA-binding peptides
    • Barrick, J. E., & Roberts, R. W. (2002). Sequence analysis of an artificial family of RNA-binding peptides. Protein Sci., 11, 2688-96.
    • (2002) Protein Sci. , vol.11 , pp. 2688-2696
    • Barrick, J.E.1    Roberts, R.W.2
  • 15
    • 0034854609 scopus 로고    scopus 로고
    • Selection of RNA-binding peptides using mRNA-peptide fusions
    • Barrick, J. E., Takahashi, T. T., Balakin, A., & Roberts, R. W. (2001). Selection of RNA-binding peptides using mRNA-peptide fusions. Methods, 23, 287-93.
    • (2001) Methods , vol.23 , pp. 287-293
    • Barrick, J.E.1    Takahashi, T.T.2    Balakin, A.3    Roberts, R.W.4
  • 16
    • 0030847064 scopus 로고    scopus 로고
    • Bacteriophage therapy and prophylaxis: rediscovery and renewed assessment of potential
    • Barrow, P. A., & Soothill, J. S. (1997). Bacteriophage therapy and prophylaxis: rediscovery and renewed assessment of potential. Trends Microbiol., 5(7), 268-71.
    • (1997) Trends Microbiol. , vol.5 , Issue.7 , pp. 268-271
    • Barrow, P.A.1    Soothill, J.S.2
  • 17
    • 0029880651 scopus 로고    scopus 로고
    • Toward cell-targeting gene therapy vectors: selection of cell-binding peptides from random peptide-presenting phage libraries
    • Barry, M. A., Dower, W. J., & Johnston, S. A. (1996). Toward cell-targeting gene therapy vectors: selection of cell-binding peptides from random peptide-presenting phage libraries. Nat. Med., 2, 299-305.
    • (1996) Nat. Med. , vol.2 , pp. 299-305
    • Barry, M.A.1    Dower, W.J.2    Johnston, S.A.3
  • 18
    • 0025678186 scopus 로고
    • Hormone phage: an enrichment method for variant proteins with altered binding properties
    • Bass, S., Green, R., & Wells, J. A. (1990). Hormone phage: an enrichment method for variant proteins with altered binding properties. Proteins: Struct. Funct. Genet., 8, 309-14.
    • (1990) Proteins: Struct. Funct. Genet. , vol.8 , pp. 309-314
    • Bass, S.1    Green, R.2    Wells, J.A.3
  • 19
    • 84896224485 scopus 로고    scopus 로고
    • Viral fibers
    • United States Patent 7332321
    • Belcher, A. M., & Lee, S.-W. (2008). Viral fibers. United States Patent 7332321.
    • (2008)
    • Belcher, A.M.1    Lee, S.-W.2
  • 20
    • 0035249432 scopus 로고    scopus 로고
    • Biotechnological applications of phage and cell display
    • Benhar, I. (2001). Biotechnological applications of phage and cell display. Biotechnol. Adv., 19, 1-33.
    • (2001) Biotechnol. Adv. , vol.19 , pp. 1-33
    • Benhar, I.1
  • 21
    • 0001783802 scopus 로고    scopus 로고
    • Selection of phage display combinatorial library peptides with affinity for a yohimbine imprinted methacrylate polymer
    • Berglund, J., Lindbladh, C., Nicholls, I. A., & Mosbach, K. (1998). Selection of phage display combinatorial library peptides with affinity for a yohimbine imprinted methacrylate polymer. Anal. Commun., 35, 3-7.
    • (1998) Anal. Commun. , vol.35 , pp. 3-7
    • Berglund, J.1    Lindbladh, C.2    Nicholls, I.A.3    Mosbach, K.4
  • 22
    • 0023922661 scopus 로고
    • Escherichia coli secretion of an active chimeric antibody fragment
    • Better, M., Chang, C. P., Robinson, R. R., & Horwitz, A.H. (1988). Escherichia coli secretion of an active chimeric antibody fragment. Science, 240, 1041-3.
    • (1988) Science , vol.240 , pp. 1041-1043
    • Better, M.1    Chang, C.P.2    Robinson, R.R.3    Horwitz, A.H.4
  • 23
    • 34248520906 scopus 로고    scopus 로고
    • A protein microarray prepared with phage-displayed antibody clones
    • Bi, Q., Cen, X., Wang, W., Zhao, X., Wang, X., Shen, T., & Zhu, S. (2007). A protein microarray prepared with phage-displayed antibody clones. Biosens. Bioelectron., 22(12), 3278-82.
    • (2007) Biosens. Bioelectron. , vol.22 , Issue.12 , pp. 3278-3282
    • Bi, Q.1    Cen, X.2    Wang, W.3    Zhao, X.4    Wang, X.5    Shen, T.6    Zhu, S.7
  • 25
    • 0042780350 scopus 로고    scopus 로고
    • Designing repeat proteins: well-expressed, soluble and stable proteins from combinatorial libraries of consensus ankyrin repeat proteins
    • Binz, H. K., Stumpp, M. T., Forrer, P., Amstutz, P., & Plückthun, A. (2003). Designing repeat proteins: well-expressed, soluble and stable proteins from combinatorial libraries of consensus ankyrin repeat proteins. J. Mol. Biol., 332, 489-503.
    • (2003) J. Mol. Biol. , vol.332 , pp. 489-503
    • Binz, H.K.1    Stumpp, M.T.2    Forrer, P.3    Amstutz, P.4    Plückthun, A.5
  • 26
    • 21444438641 scopus 로고    scopus 로고
    • Peptides selected for binding to a virulent strain of Haemophilus influenzae by phage display are bactericidal
    • Bishop-Hurley, S. L., Schmidt, F. J., Erwin, A. L., & Smith, A. L. (2005). Peptides selected for binding to a virulent strain of Haemophilus influenzae by phage display are bactericidal. Antimicrob. Agents Chemother., 49, 2972-8.
    • (2005) Antimicrob. Agents Chemother. , vol.49 , pp. 2972-2978
    • Bishop-Hurley, S.L.1    Schmidt, F.J.2    Erwin, A.L.3    Smith, A.L.4
  • 27
    • 0030948539 scopus 로고    scopus 로고
    • Real engines of creation
    • Block, S. M. (1997). Real engines of creation. Nature, 386, 217-19.
    • (1997) Nature , vol.386 , pp. 217-219
    • Block, S.M.1
  • 28
    • 0034718615 scopus 로고    scopus 로고
    • Directed evolution of antibody fragments with monovalent femtomolar antigen-binding affinity
    • Boder E. T., Midelfort K. S., & Wittrup K. D. (2000). Directed evolution of antibody fragments with monovalent femtomolar antigen-binding affinity. Proc. Nat. Acad. Sci. USA, 97(20), 10701-5.
    • (2000) Proc. Nat. Acad. Sci. USA , vol.97 , Issue.20 , pp. 10701-10705
    • Boder, E.T.1    Midelfort, K.S.2    Wittrup, K.D.3
  • 29
    • 0030994634 scopus 로고    scopus 로고
    • Yeast surface display for screening combinatorial polypeptide libraries
    • Boder, E. T., & Wittrup, K. D. (1997). Yeast surface display for screening combinatorial polypeptide libraries. Nat. Biotech., 15, 553-57.
    • (1997) Nat. Biotech. , vol.15 , pp. 553-557
    • Boder, E.T.1    Wittrup, K.D.2
  • 30
    • 2642711705 scopus 로고    scopus 로고
    • Optimal screening of surface-displayed polypeptide libraries
    • Boder, E. T., & Wittrup, K. D. (1998). Optimal screening of surface-displayed polypeptide libraries. Biotechnol. Prog., 14, 55-62.
    • (1998) Biotechnol. Prog. , vol.14 , pp. 55-62
    • Boder, E.T.1    Wittrup, K.D.2
  • 33
    • 23744441969 scopus 로고    scopus 로고
    • Thermostability of landscape phage probes
    • Brigati, J. R., & Petrenko, V. A. (2005). Thermostability of landscape phage probes. Anal. Bioanal. Chem., 382, 1346-50.
    • (2005) Anal. Bioanal. Chem. , vol.382 , pp. 1346-1350
    • Brigati, J.R.1    Petrenko, V.A.2
  • 35
    • 0033639098 scopus 로고    scopus 로고
    • A novel approach for the identification of unique tumor vasculature bonding peptides using an E. coli peptide display library
    • Brown, C. K., Modzelewski, R. A., Johnson, C. S., & Wong, M.K. (2000). A novel approach for the identification of unique tumor vasculature bonding peptides using an E. coli peptide display library. Ann. Surg. Oncol. 7(10), 743-9.
    • (2000) Ann. Surg. Oncol. , vol.7 , Issue.10 , pp. 743-749
    • Brown, C.K.1    Modzelewski, R.A.2    Johnson, C.S.3    Wong, M.K.4
  • 36
    • 0026669435 scopus 로고
    • Engineered iron oxide-adhesion mutants of the Escherichia coli phage l receptor
    • Brown, S. (1992). Engineered iron oxide-adhesion mutants of the Escherichia coli phage l receptor. Proc. Natl Acad. Sci. USA, 89, 8651-5.
    • (1992) Proc. Natl Acad. Sci. USA , vol.89 , pp. 8651-8655
    • Brown, S.1
  • 37
    • 0030969778 scopus 로고    scopus 로고
    • Metal-recognition by repeating polypeptides
    • Brown, S. (1997). Metal-recognition by repeating polypeptides. Nat. Biotechnol., 15, 269-72.
    • (1997) Nat. Biotechnol. , vol.15 , pp. 269-272
    • Brown, S.1
  • 38
    • 0034625319 scopus 로고    scopus 로고
    • Genetic analysis of crystal growth
    • Brown, S., Sarikaya, M., & Johnson, E. (2000). Genetic analysis of crystal growth. J. Mol. Biol., 299, 725-32.
    • (2000) J. Mol. Biol. , vol.299 , pp. 725-732
    • Brown, S.1    Sarikaya, M.2    Johnson, E.3
  • 40
    • 0025838698 scopus 로고
    • A large array of human monoclonal antibodies to type 1 human immunodeficiency virus from combinatorial libraries of asymptomatic individuals
    • Burton, D. R., Barbas, C. F. 3rd, Persson, M. A., Koenig, S., Chanock, R. M., & Lerner, R. A. (1991). A large array of human monoclonal antibodies to type 1 human immunodeficiency virus from combinatorial libraries of asymptomatic individuals. Proc. Natl. Acad. Sci. USA, 88, 10134-7.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 10134-10137
    • Burton, D.R.1    Barbas III, C.F.2    Persson, M.A.3    Koenig, S.4    Chanock, R.M.5    Lerner, R.A.6
  • 41
    • 0029616481 scopus 로고
    • Monovalent phage display of human interleukin (hIL)-6: Selection of superbinder variants from a complex molecular repertoire in the hIL-6 D-helix
    • Cabibbo, A., Sporeno, E., Toniatti, C., Altamura, S., Savino, R., Paonessa, G., & Ciliberto, G. (1995). Monovalent phage display of human interleukin (hIL)-6: Selection of superbinder variants from a complex molecular repertoire in the hIL-6 D-helix. Gene, 167, 41-7.
    • (1995) Gene , vol.167 , pp. 41-47
    • Cabibbo, A.1    Sporeno, E.2    Toniatti, C.3    Altamura, S.4    Savino, R.5    Paonessa, G.6    Ciliberto, G.7
  • 42
    • 0029021085 scopus 로고
    • Anti-melanoma antibodies from melanoma patients immunized with genetically modified antilogous tumor cells: selection of specific antibodies from single-chain Fv fusion phage libraries
    • Cai, X., & Garen, A. (1995). Anti-melanoma antibodies from melanoma patients immunized with genetically modified antilogous tumor cells: selection of specific antibodies from single-chain Fv fusion phage libraries. Proc. Natl. Acad. Sci. USA, 92, 6537-41.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 6537-6541
    • Cai, X.1    Garen, A.2
  • 44
    • 38749100531 scopus 로고    scopus 로고
    • Specific and selective probes for Pseudomonas aeruginosa from phage-displayed random peptide libraries
    • Carnazza, S., Foti, C., Gioffrè, G., Felici, F., & Guglielmino, S. (2008). Specific and selective probes for Pseudomonas aeruginosa from phage-displayed random peptide libraries. Bios. Bioelectron., 23, 1137-44.
    • (2008) Bios. Bioelectron. , vol.23 , pp. 1137-1144
    • Carnazza, S.1    Foti, C.2    Gioffrè, G.3    Felici, F.4    Guglielmino, S.5
  • 47
    • 0025718897 scopus 로고
    • Expression of antibody Fab domains on bacteriophage surfaces
    • Chang, C. N., Landolfi, N. F., & Queen, C. (1991). Expression of antibody Fab domains on bacteriophage surfaces. J. Immunology, 147, 3610-4.
    • (1991) J. Immunology , vol.147 , pp. 3610-3614
    • Chang, C.N.1    Landolfi, N.F.2    Queen, C.3
  • 48
    • 33845633382 scopus 로고    scopus 로고
    • Eliminating helper phage from phage display
    • Epub 2006 Nov 6
    • Chasteen, L., Ayriss, J., Pavlik, P., & Bradbury, A. R. (2006). Eliminating helper phage from phage display. Nucleic Acids Res., 34(21), e145 [Epub 2006 Nov 6].
    • (2006) Nucleic Acids Res. , vol.34 , Issue.21
    • Chasteen, L.1    Ayriss, J.2    Pavlik, P.3    Bradbury, A.R.4
  • 49
    • 0032167918 scopus 로고    scopus 로고
    • Antigenicity of fullerenes: antibodies specific for fullerenes and their characteristics
    • Chen, B. X., Wilson, S. R., Das, M., Coughlin, D. J., & Erlanger, B. F. (1998). Antigenicity of fullerenes: antibodies specific for fullerenes and their characteristics. Proc. Natl. Acad. Sci. USA, 95, 10809-13.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 10809-10813
    • Chen, B.X.1    Wilson, S.R.2    Das, M.3    Coughlin, D.J.4    Erlanger, B.F.5
  • 50
    • 84891964880 scopus 로고    scopus 로고
    • Novel approach to generate human monoclonal antibodies by PROfusionTM Technology
    • Cambridge Healthtech Institute 4th Annual Conference on Recombinant Antibodies. Cambridge, MA, USA
    • Chen, Y. (2003). Novel approach to generate human monoclonal antibodies by PROfusionTM Technology. Cambridge Healthtech Institute 4th Annual Conference on Recombinant Antibodies. Cambridge, MA, USA.
    • (2003)
    • Chen, Y.1
  • 51
    • 0029934724 scopus 로고    scopus 로고
    • Identification of a biologically significant DNA-binding peptide motif by use of a random phage display library
    • Cheng, X., Kay, B. K., & Juliano, R. L. (1996). Identification of a biologically significant DNA-binding peptide motif by use of a random phage display library. Gene, 171, 1-8.
    • (1996) Gene , vol.171 , pp. 1-8
    • Cheng, X.1    Kay, B.K.2    Juliano, R.L.3
  • 52
    • 0024561993 scopus 로고
    • Direct cDNA cloning of the rearranged immunoglobulin variable region
    • Chiang, Y. L., Sheng-Dong, R., Brow, M. A., & Larrick, J. W. (1989). Direct cDNA cloning of the rearranged immunoglobulin variable region. Biotechniques, 7, 360-6.
    • (1989) Biotechniques , vol.7 , pp. 360-366
    • Chiang, Y.L.1    Sheng-Dong, R.2    Brow, M.A.3    Larrick, J.W.4
  • 53
    • 33748483510 scopus 로고    scopus 로고
    • Investigation of de novo totally random biosequences. Part I. A general method for in vitro selection of folded domains from a random polypeptide library displayed on phage
    • Chiarabelli, C., Vrijbloed, J. W., Thomas, R. M., & Luisi, P. L. (2006a). Investigation of de novo totally random biosequences. Part I. A general method for in vitro selection of folded domains from a random polypeptide library displayed on phage. Chem. Biodiv., 3, 827-39.
    • (2006) Chem. Biodiv. , vol.3 , pp. 827-839
    • Chiarabelli, C.1    Vrijbloed, J.W.2    Thomas, R.M.3    Luisi, P.L.4
  • 54
    • 33748541979 scopus 로고    scopus 로고
    • Investigation of de novo totally random biosequences. Part II. On the folding frequency in a totally random library of de novo proteins obtained by phage display
    • Chiarabelli, C., Vrijbloed, J. W., De Lucrezia, D., Thomas, R. M., Stano, P., Polticelli, F., Ottone, T., Papa, E., & Luisi, P. L. (2006b). Investigation of de novo totally random biosequences. Part II. On the folding frequency in a totally random library of de novo proteins obtained by phage display. Chem. Biodiv., 3, 840-59.
    • (2006) Chem. Biodiv. , vol.3 , pp. 840-859
    • Chiarabelli, C.1    Vrijbloed, J.W.2    De Lucrezia, D.3    Thomas, R.M.4    Stano, P.5    Polticelli, F.6    Ottone, T.7    Papa, E.8    Luisi, P.L.9
  • 55
    • 33845262706 scopus 로고    scopus 로고
    • Engineering life through Synthetic Biology
    • Chopra, P., & Kamma, A. (2006). Engineering life through Synthetic Biology. In Silico Biology, 6, 401-10.
    • (2006) In Silico Biology , vol.6 , pp. 401-410
    • Chopra, P.1    Kamma, A.2
  • 56
    • 0036359197 scopus 로고    scopus 로고
    • Targeting random mutations to hotspots in antibody variable domains for affinity improvement
    • In P. M. O'Brien, & R. Aitken (Eds.), Totowa, NJ: Humana Press
    • Chowdhury, P. S. (2002). Targeting random mutations to hotspots in antibody variable domains for affinity improvement. In P. M. O'Brien, & R. Aitken (Eds.), Antibody Phage Display: Methods and Protocols. (pp. 269-86). Totowa, NJ: Humana Press.
    • (2002) Antibody Phage Display: Methods and Protocols. , pp. 269-286
    • Chowdhury, P.S.1
  • 57
    • 0025835310 scopus 로고
    • Making antibody fragments using phage display libraries
    • Clackson, T., Hoogenboom, H. R., Griffiths, A. D., & Winter, G. (1991). Making antibody fragments using phage display libraries. Nature, 352, 624-8.
    • (1991) Nature , vol.352 , pp. 624-628
    • Clackson, T.1    Hoogenboom, H.R.2    Griffiths, A.D.3    Winter, G.4
  • 58
    • 4043168481 scopus 로고    scopus 로고
    • Bacterial viruses as human vaccines?
    • Clark, J. R., & March, J. B. (2004a). Bacterial viruses as human vaccines? Expert Rev. Vaccines, 3, 463-76.
    • (2004) Expert Rev. Vaccines , vol.3 , pp. 463-476
    • Clark, J.R.1    March, J.B.2
  • 59
    • 0347090561 scopus 로고    scopus 로고
    • Bacteriophage-mediated nucleic acid immunization
    • Clark, J. R., & March, J. B. (2004b). Bacteriophage-mediated nucleic acid immunization. FEMS Immunol. Med. Microbiol., 40, 21-6.
    • (2004) FEMS Immunol. Med. Microbiol. , vol.40 , pp. 21-26
    • Clark, J.R.1    March, J.B.2
  • 60
    • 33646596612 scopus 로고    scopus 로고
    • Bacteriophages and biotechnology: vaccines, gene therapy and antibacterials
    • Clark, J. R., & March, J. B. (2006). Bacteriophages and biotechnology: vaccines, gene therapy and antibacterials. Trends Biotech., 24, 212-8.
    • (2006) Trends Biotech. , vol.24 , pp. 212-218
    • Clark, J.R.1    March, J.B.2
  • 61
    • 0035183986 scopus 로고    scopus 로고
    • Rapid and precise epitope mapping of monoclonal antibodies against Plasmodium falciparum AMA1 by combined phage display of fragments and random peptides
    • Coley, A. M., Campanale, N. V., Casey, J. L., Hodder, A. N., Crewther, P. E., Anders, R. F., Tilley, L. M., & Foley, M. (2001). Rapid and precise epitope mapping of monoclonal antibodies against Plasmodium falciparum AMA1 by combined phage display of fragments and random peptides. Protein Eng., 14, 691-8.
    • (2001) Protein Eng. , vol.14 , pp. 691-698
    • Coley, A.M.1    Campanale, N.V.2    Casey, J.L.3    Hodder, A.N.4    Crewther, P.E.5    Anders, R.F.6    Tilley, L.M.7    Foley, M.8
  • 63
    • 0035948965 scopus 로고    scopus 로고
    • Electrochemical deposition and characterization of conducting polymer polypyrrole/PSS on multichannel neural probes
    • Cui, X., Hetke, J. F., Wiler, J. A., Anderson, D. J., & Martin, D. C. (2001). Electrochemical deposition and characterization of conducting polymer polypyrrole/PSS on multichannel neural probes. Sensors Actuat. A, 93, 8-18.
    • (2001) Sensors Actuat. A , vol.93 , pp. 8-18
    • Cui, X.1    Hetke, J.F.2    Wiler, J.A.3    Anderson, D.J.4    Martin, D.C.5
  • 64
    • 0036008852 scopus 로고    scopus 로고
    • Selection of v-abl tyrosine kinase substrate sequences from randomized peptide and cellular proteomic libraries using mRNA display
    • Cujec, T. P., Medeiros, P. F., Hammond, P., Rise, C., & Kreider, B. L. (2002). Selection of v-abl tyrosine kinase substrate sequences from randomized peptide and cellular proteomic libraries using mRNA display. Chem. Biol., 9, 253-264.
    • (2002) Chem. Biol. , vol.9 , pp. 253-264
    • Cujec, T.P.1    Medeiros, P.F.2    Hammond, P.3    Rise, C.4    Kreider, B.L.5
  • 66
  • 68
    • 33748487616 scopus 로고    scopus 로고
    • Investigation of de novo totally random biosequences. Part III. RNA foster: a novel assay to investigate RNA folding structural properties
    • De Lucrezia, D., Franchi, M., Chiarabelli, C., Gallori, E., & Luisi, P. L. (2006a). Investigation of de novo totally random biosequences. Part III. RNA foster: a novel assay to investigate RNA folding structural properties. Chem. Biodiv., 3, 860-8.
    • (2006) Chem. Biodiv. , vol.3 , pp. 860-868
    • De Lucrezia, D.1    Franchi, M.2    Chiarabelli, C.3    Gallori, E.4    Luisi, P.L.5
  • 69
    • 33748517635 scopus 로고    scopus 로고
    • Investigation of de novo totally random biosequences. Part IV. Folding properties of de novo, totally random RNAs
    • De Lucrezia, D., Franchi, M., Chiarabelli, C., Gallori, E., & Luisi, P. L. (2006b). Investigation of de novo totally random biosequences. Part IV. Folding properties of de novo, totally random RNAs. Chem. Biodiv., 3, 869-77.
    • (2006) Chem. Biodiv. , vol.3 , pp. 869-877
    • De Lucrezia, D.1    Franchi, M.2    Chiarabelli, C.3    Gallori, E.4    Luisi, P.L.5
  • 70
    • 0031097510 scopus 로고    scopus 로고
    • Polypeptide materials: new synthetic methods and applications
    • Deming, T. J. (1997). Polypeptide materials: new synthetic methods and applications. Adv. Mater., 9, 299-311.
    • (1997) Adv. Mater. , vol.9 , pp. 299-311
    • Deming, T.J.1
  • 71
    • 0028339940 scopus 로고
    • Selection of antibody single-chain variable fragments with improved carbohydrate binding by phage display
    • Deng, S. J., MacKenzie, C. R., Sadowska, J., Michniewicz, J., Young, N. M., Bundle, D. R., & Narang, S. A. (1994). Selection of antibody single-chain variable fragments with improved carbohydrate binding by phage display. J. Biol. Chem., 269, 9533-8.
    • (1994) J. Biol. Chem. , vol.269 , pp. 9533-9538
    • Deng, S.J.1    MacKenzie, C.R.2    Sadowska, J.3    Michniewicz, J.4    Young, N.M.5    Bundle, D.R.6    Narang, S.A.7
  • 74
    • 21044431604 scopus 로고    scopus 로고
    • Bacteriophage-mediated protein delivery into the central nervous system and its application in immunopharmacotherapy
    • Dickerson, T. J., Kaufmann, G. F., & Janda, K. D. (2005). Bacteriophage-mediated protein delivery into the central nervous system and its application in immunopharmacotherapy. Expert Opin. Biol. Ther., 5, 773-81.
    • (2005) Expert Opin. Biol. Ther. , vol.5 , pp. 773-781
    • Dickerson, T.J.1    Kaufmann, G.F.2    Janda, K.D.3
  • 75
    • 0035880583 scopus 로고    scopus 로고
    • Direct and quantitative detection of bacteriophage by "hearing" surface detachment using a quartz crystal microbalance
    • Dultsev, F. N., Speight, R. E., Fiorini, M. T., Blackburn, J. M., Abell, C., Ostanin, V. P., & Klenerman, D. (2001). Direct and quantitative detection of bacteriophage by "hearing" surface detachment using a quartz crystal microbalance. Anal. Chem., 73(16), 3935-9.
    • (2001) Anal. Chem. , vol.73 , Issue.16 , pp. 3935-3939
    • Dultsev, F.N.1    Speight, R.E.2    Fiorini, M.T.3    Blackburn, J.M.4    Abell, C.5    Ostanin, V.P.6    Klenerman, D.7
  • 76
    • 0030455082 scopus 로고    scopus 로고
    • Mammalian cell binding and transfection mediated by surface-modified bacteriophage lambda
    • Dunn, I. S. (1996). Mammalian cell binding and transfection mediated by surface-modified bacteriophage lambda. Biochimie, 78, 856-61.
    • (1996) Biochimie , vol.78 , pp. 856-861
    • Dunn, I.S.1
  • 77
    • 3042655537 scopus 로고    scopus 로고
    • Computational design of a biologically active enzyme
    • Dwyer, M. A., Looger, L. L., & Hellinga, H. W. (2004). Computational design of a biologically active enzyme. Science, 304, 1967-71.
    • (2004) Science , vol.304 , pp. 1967-1971
    • Dwyer, M.A.1    Looger, L.L.2    Hellinga, H.W.3
  • 78
    • 0344012535 scopus 로고    scopus 로고
    • A vascular endothelial growth factor high affinity receptor 1-specific peptide with antiangiogenic activity identified using a phage display peptide library
    • El-Mousawi, M., Tchistiakova, L., Yurchenko, L., Pietrzynski, G., Moreno, M., Stanimirovic, D., Ahmad, D., & Alakhov, V. (2003). A vascular endothelial growth factor high affinity receptor 1-specific peptide with antiangiogenic activity identified using a phage display peptide library. J. Biol. Chem., 278, 46681-91.
    • (2003) J. Biol. Chem. , vol.278 , pp. 46681-46691
    • El-Mousawi, M.1    Tchistiakova, L.2    Yurchenko, L.3    Pietrzynski, G.4    Moreno, M.5    Stanimirovic, D.6    Ahmad, D.7    Alakhov, V.8
  • 79
    • 0030596493 scopus 로고    scopus 로고
    • Directing antigen specificity towards botulinum neurotoxin with combinatorial phage display libraries
    • Emanuel, P., O'Brien, T., Burans, J., DasGupta, B. R., Valdes, J. J., & Eldefrawi, M. (1996). Directing antigen specificity towards botulinum neurotoxin with combinatorial phage display libraries. J. Immunol. Methods, 193, 189-97.
    • (1996) J. Immunol. Methods , vol.193 , pp. 189-197
    • Emanuel, P.1    O'Brien, T.2    Burans, J.3    DasGupta, B.R.4    Valdes, J.J.5    Eldefrawi, M.6
  • 80
    • 0002461546 scopus 로고    scopus 로고
    • Binding of an anti-fullerene IgG monoclonal antibody to single wall carbon nanotubes
    • Erlanger, B. F., Chen, B.-X., Zhu, M., & Brus, L. (2001). Binding of an anti-fullerene IgG monoclonal antibody to single wall carbon nanotubes. Nano Lett., 1, 465-7.
    • (2001) Nano Lett. , vol.1 , pp. 465-467
    • Erlanger, B.F.1    Chen, B.-X.2    Zhu, M.3    Brus, L.4
  • 82
    • 1842857805 scopus 로고    scopus 로고
    • Flow cytometric screening of yeast surface display libraries
    • Feldhaus, M. J., & Siegel, R. W. (2004a). Flow cytometric screening of yeast surface display libraries. Methods Mol. Biol., 263, 311-32.
    • (2004) Methods Mol. Biol. , vol.263 , pp. 311-332
    • Feldhaus, M.J.1    Siegel, R.W.2
  • 83
    • 3142682191 scopus 로고    scopus 로고
    • Yeast display of antibody fragments: A discovery and characterization platform
    • Feldhaus, M. J., & Siegel, R. W. (2004b). Yeast display of antibody fragments: A discovery and characterization platform. J. Immunol. Methods, 290, 69-80.
    • (2004) J. Immunol. Methods , vol.290 , pp. 69-80
    • Feldhaus, M.J.1    Siegel, R.W.2
  • 84
    • 0029418639 scopus 로고
    • Peptide and protein display on the surface of filamentous bacteriophage
    • Amsterdam, The Netherlands: Elsevier Science B.V. In M. R. El-Gewely (Ed.)
    • Felici, F., Luzzago, A., Monaci, P., Nicosia, A., Sollazzo, M., & Traboni, C. (1995). Peptide and protein display on the surface of filamentous bacteriophage. In M. R. El-Gewely (Ed.), Biotechnology Annual Review (Volume 1, 149-83). Amsterdam, The Netherlands: Elsevier Science B.V.
    • (1995) Biotechnology Annual Review , vol.1 , pp. 149-183
    • Felici, F.1    Luzzago, A.2    Monaci, P.3    Nicosia, A.4    Sollazzo, M.5    Traboni, C.6
  • 85
    • 0033533503 scopus 로고    scopus 로고
    • Core-directed protein design. I. An experimental method for selecting stable proteins from combinatorial libraries
    • Finucane, M. D., Tuna, M., Lees, J. H., & Woolfson, D. N. (1999). Core-directed protein design. I. An experimental method for selecting stable proteins from combinatorial libraries. Biochemistry, 38, 11604-12.
    • (1999) Biochemistry , vol.38 , pp. 11604-11612
    • Finucane, M.D.1    Tuna, M.2    Lees, J.H.3    Woolfson, D.N.4
  • 86
    • 0142042549 scopus 로고    scopus 로고
    • Synthesis and organization of nanoscale semiconductor materials using evolved peptide specificity and viral capsid assembly
    • Flynn, C. E., Mao, C., Hayhurst, A., Williams, J. L., Georgiou, G., Iversona B., & Belcher, A. M. (2003). Synthesis and organization of nanoscale semiconductor materials using evolved peptide specificity and viral capsid assembly. J. Mater. Chem., 13, 2414-21.
    • (2003) J. Mater. Chem. , vol.13 , pp. 2414-2421
    • Flynn, C.E.1    Mao, C.2    Hayhurst, A.3    Williams, J.L.4    Georgiou, G.5    Iversona, B.6    Belcher, A.M.7
  • 87
    • 0028216366 scopus 로고
    • A general strategy to identify mimotopes of pathological antigens using only random peptide libraries and human sera
    • Folgori, A., Tafi, R., Meola, A., Felici, F., Galfré, G., Cortese, R., Monaci, P., & Nicosia, A. (1994). A general strategy to identify mimotopes of pathological antigens using only random peptide libraries and human sera. EMBO J., 13, 2236-43.
    • (1994) EMBO J. , vol.13 , pp. 2236-2243
    • Folgori, A.1    Tafi, R.2    Meola, A.3    Felici, F.4    Galfré, G.5    Cortese, R.6    Monaci, P.7    Nicosia, A.8
  • 88
    • 0027425230 scopus 로고
    • Production and fluorescence-activated cell sorting of Escherichia coli expressing a functional antibody fragment on the external surface
    • Francisco, J. A., Campbell, R., Iverson, B. L., & Georgiou, G. (1993). Production and fluorescence-activated cell sorting of Escherichia coli expressing a functional antibody fragment on the external surface. Proc. Nat. Acad. Sci. USA, 90, 10444-8.
    • (1993) Proc. Nat. Acad. Sci. USA , vol.90 , pp. 10444-10448
    • Francisco, J.A.1    Campbell, R.2    Iverson, B.L.3    Georgiou, G.4
  • 89
    • 36849066165 scopus 로고    scopus 로고
    • Magnetostrictive microcantilever as an advanced transducer for biosensors
    • Fu, L., Li, S., Zhang, K., Chen, I.-H., Petrenko, V. A., & Cheng, Z. (2007). Magnetostrictive microcantilever as an advanced transducer for biosensors. Sensors J., 7, 2929-41.
    • (2007) Sensors J. , vol.7 , pp. 2929-2941
    • Fu, L.1    Li, S.2    Zhang, K.3    Chen, I.-H.4    Petrenko, V.A.5    Cheng, Z.6
  • 91
    • 0031012062 scopus 로고    scopus 로고
    • Display of heterologous proteins on the surface of microorganisms: from the screening of combinatorial libraries to live recombinant vaccines
    • Georgiou, G., Stathopoulos, C., Daugherty, P. S., Nayak, A. R., Iverson, B. L., & Curtis, R. III. (1997). Display of heterologous proteins on the surface of microorganisms: from the screening of combinatorial libraries to live recombinant vaccines. Nat. Biotech., 15, 29-34.
    • (1997) Nat. Biotech. , vol.15 , pp. 29-34
    • Georgiou, G.1    Stathopoulos, C.2    Daugherty, P.S.3    Nayak, A.R.4    Iverson, B.L.5    Curtis III, R.6
  • 92
    • 0022646579 scopus 로고
    • A priori delineation of a peptide which mimics a discontinuous antigenic determinant
    • Geysen, H. M., Rodda, S. J., & Mason, T. J. (1986a). A priori delineation of a peptide which mimics a discontinuous antigenic determinant. Mol. Immunol., 23, 709-15.
    • (1986) Mol. Immunol. , vol.23 , pp. 709-715
    • Geysen, H.M.1    Rodda, S.J.2    Mason, T.J.3
  • 93
    • 0022482579 scopus 로고
    • The delineation of peptides able to mimic assembled epitopes
    • Geysen, H. M., Rodda, S. J., & Mason, T. J. (1986b). The delineation of peptides able to mimic assembled epitopes. Ciba Found. Symp., 119, 130-49.
    • (1986) Ciba Found. Symp. , vol.119 , pp. 130-149
    • Geysen, H.M.1    Rodda, S.J.2    Mason, T.J.3
  • 95
    • 0035942159 scopus 로고    scopus 로고
    • mRNA display: diversity matters during in vitro selection
    • Gold, L. (2001). mRNA display: diversity matters during in vitro selection. Proc. Natl. Acad. Sci. USA, 98(9), 4825-6.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , Issue.9 , pp. 4825-4826
    • Gold, L.1
  • 97
    • 0032951910 scopus 로고    scopus 로고
    • Selection of phage-display peptides that bind to cucumber mosaic virus coat protein
    • Gough, K.C., Cockburn, W., & Whitelam, G.C. (1999). Selection of phage-display peptides that bind to cucumber mosaic virus coat protein. J. Virol. Methods, 79, 169-80.
    • (1999) J. Virol. Methods , vol.79 , pp. 169-180
    • Gough, K.C.1    Cockburn, W.2    Whitelam, G.C.3
  • 99
    • 0031568670 scopus 로고    scopus 로고
    • Human anti-nicotinic acetylcholine receptor recombinant Fab fragments isolated from thymus-derived phage display libraries from myasthenia gravis patients reflect predominant specificities in serum and block the action of pathogenic serum antibodies
    • Graus, Y. F., de Baets, M. H., Parren, P. W., Berrih-Aknin, S., Wokke, J., van Breda Vriesman, P. J., & Burton, D. R. (1997). Human anti-nicotinic acetylcholine receptor recombinant Fab fragments isolated from thymus-derived phage display libraries from myasthenia gravis patients reflect predominant specificities in serum and block the action of pathogenic serum antibodies. J. Immunol., 158, 1919-29.
    • (1997) J. Immunol. , vol.158 , pp. 1919-1929
    • Graus, Y.F.1    de Baets, M.H.2    Parren, P.W.3    Berrih-Aknin, S.4    Wokke, J.5    van Breda Vriesman, P.J.6    Burton, D.R.7
  • 100
    • 0025899542 scopus 로고
    • Multiple display of foreign peptides on a filamentous bacteriophage
    • Greenwood, J., Willis, A.E., & Perham, R.N. (1991). Multiple display of foreign peptides on a filamentous bacteriophage. J. Mol. Biol., 220, 821-7.
    • (1991) J. Mol. Biol. , vol.220 , pp. 821-827
    • Greenwood, J.1    Willis, A.E.2    Perham, R.N.3
  • 101
    • 0031933840 scopus 로고    scopus 로고
    • Strategies for selection of antibodies by phage display
    • Griffiths, A. D., & Duncan, A. R. (1998). Strategies for selection of antibodies by phage display. Curr. Opin. Biotechnol., 9, 102-8.
    • (1998) Curr. Opin. Biotechnol. , vol.9 , pp. 102-108
    • Griffiths, A.D.1    Duncan, A.R.2
  • 102
    • 0029004982 scopus 로고
    • A phage display system for studying the sequence determinants of protein-folding
    • Gu, H. D., Yi, Q. A., Bray, S. T., Riddle, D. S., Shiau, A. K., & Baker, D. (1995). A phage display system for studying the sequence determinants of protein-folding. Protein Science, 4, 1108-17.
    • (1995) Protein Science , vol.4 , pp. 1108-1117
    • Gu, H.D.1    Yi, Q.A.2    Bray, S.T.3    Riddle, D.S.4    Shiau, A.K.5    Baker, D.6
  • 105
    • 0035877791 scopus 로고    scopus 로고
    • In vitro selection and characterization of Bcl-X(L)-binding proteins from a mix of tissue-specific mRNA display libraries
    • Hammond, P. W., Alpin, J., Rise, C. E., Wright, M., & Kreider, B. L. (2001). In vitro selection and characterization of Bcl-X(L)-binding proteins from a mix of tissue-specific mRNA display libraries. J. Biol. Chem., 276, 20898-906.
    • (2001) J. Biol. Chem. , vol.276 , pp. 20898-20906
    • Hammond, P.W.1    Alpin, J.2    Rise, C.E.3    Wright, M.4    Kreider, B.L.5
  • 106
    • 0030974119 scopus 로고    scopus 로고
    • In vitro selection and evolution of functional proteins using ribosome display
    • Hanes, J., & Plückthun, A. (1997). In vitro selection and evolution of functional proteins using ribosome display. Proc. Natl. Acad. Sci. USA, 94, 4937-42.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 4937-4942
    • Hanes, J.1    Plückthun, A.2
  • 107
    • 0033733267 scopus 로고    scopus 로고
    • Selecting and evolving functional proteins in vitro by ribosome display
    • Hanes, J., Jermutus, L., & Plückthun, A. (2000a). Selecting and evolving functional proteins in vitro by ribosome display. Methods Enzymol., 328, 404-30.
    • (2000) Methods Enzymol. , vol.328 , pp. 404-430
    • Hanes, J.1    Jermutus, L.2    Plückthun, A.3
  • 108
    • 0033664270 scopus 로고    scopus 로고
    • Picomolar affinity antibodies from a fully synthetic naïve library selected and evolved by ribosome display
    • Hanes, J., Schaffitzel, C., Knappik, A., & Plückthun, A. (2000b). Picomolar affinity antibodies from a fully synthetic naïve library selected and evolved by ribosome display. Nat. Biotechnol., 18, 1287-92.
    • (2000) Nat. Biotechnol. , vol.18 , pp. 1287-1292
    • Hanes, J.1    Schaffitzel, C.2    Knappik, A.3    Plückthun, A.4
  • 109
    • 0031574037 scopus 로고    scopus 로고
    • Antibody-ribosome-mRNA (ARM) complexes as efficient selection particles for in vitro display and evolution of antibody combining sites
    • He, M., & Taussig, M. J. (1997). Antibody-ribosome-mRNA (ARM) complexes as efficient selection particles for in vitro display and evolution of antibody combining sites. Nucleic Acids Res., 25, 5132-4.
    • (1997) Nucleic Acids Res. , vol.25 , pp. 5132-5134
    • He, M.1    Taussig, M.J.2
  • 110
    • 33847630761 scopus 로고    scopus 로고
    • Eukaryotic Ribosome Display with in situ DNA recovery
    • He, M., & Taussig, M. J. (2007). Eukaryotic Ribosome Display with in situ DNA recovery. Nat. Methods, 4, 281-8.
    • (2007) Nat. Methods , vol.4 , pp. 281-288
    • He, M.1    Taussig, M.J.2
  • 111
    • 0037443427 scopus 로고    scopus 로고
    • Peptide G protein agonists from a phage display library
    • Hessling, J., Lohse, M. J., & Klotz, K. N. (2003). Peptide G protein agonists from a phage display library. Biochem. Pharmacol., 65, 961-7.
    • (2003) Biochem. Pharmacol. , vol.65 , pp. 961-967
    • Hessling, J.1    Lohse, M.J.2    Klotz, K.N.3
  • 112
    • 7244261722 scopus 로고    scopus 로고
    • Phage antibody chip for discriminating proteomes from different cells
    • Hong, L., Liao, W., Zhao, X. S., & Zhu, S. G. (2004). Phage antibody chip for discriminating proteomes from different cells. Acta Phys.-Chim. Sin., 20, 1182-5.
    • (2004) Acta Phys.-Chim. Sin. , vol.20 , pp. 1182-1185
    • Hong, L.1    Liao, W.2    Zhao, X.S.3    Zhu, S.G.4
  • 113
    • 0031081318 scopus 로고    scopus 로고
    • Designing and optimizing library selection strategies for generating high-affinity antibodies
    • Hoogenboom, H. R. (1997). Designing and optimizing library selection strategies for generating high-affinity antibodies. Trends Biotechnol., 15, 62-70.
    • (1997) Trends Biotechnol. , vol.15 , pp. 62-70
    • Hoogenboom, H.R.1
  • 114
    • 0033853776 scopus 로고    scopus 로고
    • Natural and designer binding sites made by phage display technology
    • Hoogenboom, H. R., & Chames, P. (2000). Natural and designer binding sites made by phage display technology. Immunol. Today, 21, 371-8.
    • (2000) Immunol. Today , vol.21 , pp. 371-378
    • Hoogenboom, H.R.1    Chames, P.2
  • 116
    • 0025740577 scopus 로고
    • Multi-subunit proteins on the surface of filamentous phage: methodologies for displaying antibody (Fab) heavy and light chains
    • Hoogenboom, H. R., Griffiths, A. D., Johnson, K. S., Chiswell, D. J., Hudson, P., & Winter, G. (1991). Multi-subunit proteins on the surface of filamentous phage: methodologies for displaying antibody (Fab) heavy and light chains. Nucl. Acids Res., 19, 4133-7.
    • (1991) Nucl. 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
  • 117
    • 1642314171 scopus 로고    scopus 로고
    • Interior surface modification of bacteriophage MS2
    • Hooker, J. M., Kovacs, E. W., & Francis, M. B. (2004). Interior surface modification of bacteriophage MS2. J. Am. Chem. Soc., 126, 3718-9.
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 3718-3719
    • Hooker, J.M.1    Kovacs, E.W.2    Francis, M.B.3
  • 119
    • 23144466183 scopus 로고    scopus 로고
    • Programmable assembly of nanoarchitectures using genetically engineered viruses
    • Huang, Y., Chiang, C.-Y., Lee, S. K., Gao, Y., Hu, E. L., De Yoreo, J., & Belcher, A. M. (2005). Programmable assembly of nanoarchitectures using genetically engineered viruses. Nano Letters, 5(7), 1429-34.
    • (2005) Nano Letters , vol.5 , Issue.7 , pp. 1429-1434
    • Huang, Y.1    Chiang, C.-Y.2    Lee, S.K.3    Gao, Y.4    Hu, E.L.5    De Yoreo, J.6    Belcher, A.M.7
  • 121
    • 0346158535 scopus 로고    scopus 로고
    • Mating antibody phage display with proteomics
    • Hust, M., & Dubel, S. (2004). Mating antibody phage display with proteomics. Trends in Biotechnology, 22, 8-14
    • (2004) Trends in Biotechnology , vol.22 , pp. 8-14
    • Hust, M.1    Dubel, S.2
  • 123
    • 0034351350 scopus 로고    scopus 로고
    • A review of molecular recognition technologies for detection of biological threat agents
    • Iqbal, S. S., Mayo, M. W., Bruno, J. G., Bronk, B. V., Batt, C. A., & Chambers, J. P. (2000). A review of molecular recognition technologies for detection of biological threat agents. Biosens. Bioelectron., 15, 549-78.
    • (2000) Biosens. Bioelectron. , vol.15 , pp. 549-578
    • Iqbal, S.S.1    Mayo, M.W.2    Bruno, J.G.3    Bronk, B.V.4    Batt, C.A.5    Chambers, J.P.6
  • 124
    • 0035251462 scopus 로고    scopus 로고
    • Ribosome display and affinity maturation: from antibodies to single V-domains and steps towards cancer therapeutics
    • Irving, R. A., Coia, G., Roberts, A., Nuttall, S. D., & Hudson, P. J. (2001). Ribosome display and affinity maturation: from antibodies to single V-domains and steps towards cancer therapeutics. J. Immunol. Methods, 248, 31-45.
    • (2001) J. Immunol. Methods , vol.248 , pp. 31-45
    • Irving, R.A.1    Coia, G.2    Roberts, A.3    Nuttall, S.D.4    Hudson, P.J.5
  • 125
    • 0034695430 scopus 로고    scopus 로고
    • Engineered zinc finger proteins that respond to DNA modification by HaeII and HhaI methyltransferase enzymes
    • Isalan, M., & Choo, Y. (2000). Engineered zinc finger proteins that respond to DNA modification by HaeII and HhaI methyltransferase enzymes. J. Mol. Biol., 295, 471-7.
    • (2000) J. Mol. Biol. , vol.295 , pp. 471-477
    • Isalan, M.1    Choo, Y.2
  • 126
    • 0032931995 scopus 로고    scopus 로고
    • Targeted delivery of multivalent phage display vectors into mammalian cells
    • Ivanenkov, V. V., Felici, F., & Menon, A. G. (1999). Targeted delivery of multivalent phage display vectors into mammalian cells. Biochim. Biophys. Acta, 1448(3), 463-72.
    • (1999) Biochim. Biophys. Acta , vol.1448 , Issue.3 , pp. 463-472
    • Ivanenkov, V.V.1    Felici, F.2    Menon, A.G.3
  • 127
    • 0034675350 scopus 로고    scopus 로고
    • Peptide-mediated transcytosis of phage display vectors in MDCK cells
    • Ivanenkov, V. V., & Menon, A. G. (2000). Peptide-mediated transcytosis of phage display vectors in MDCK cells. Biochem. Biophys. Res. Commun., 276, 251-7.
    • (2000) Biochem. Biophys. Res. Commun. , vol.276 , pp. 251-257
    • Ivanenkov, V.V.1    Menon, A.G.2
  • 128
    • 0032164442 scopus 로고    scopus 로고
    • Pattern recognition of antibodies for two-dimensional arrays of molecules
    • Izhaky, D., & Addadi, L. (1998). Pattern recognition of antibodies for two-dimensional arrays of molecules. Adv. Mater., 10, 1009-13.
    • (1998) Adv. Mater. , vol.10 , pp. 1009-1013
    • Izhaky, D.1    Addadi, L.2
  • 129
    • 2942562254 scopus 로고    scopus 로고
    • Bacteriophage lambda is a highly stable DNA vaccine delivery vehicle
    • Jepson, C. D., & March, J. B. (2004). Bacteriophage lambda is a highly stable DNA vaccine delivery vehicle. Vaccine, 22, 2413-9.
    • (2004) Vaccine , vol.22 , pp. 2413-2419
    • Jepson, C.D.1    March, J.B.2
  • 132
    • 0033517780 scopus 로고    scopus 로고
    • Genetic selection of phage engineered for receptor-mediated gene transfer to mammalian cells
    • Kassner, P. D., Burg, M. A., Baird, A., & Larocca D. (1999). Genetic selection of phage engineered for receptor-mediated gene transfer to mammalian cells. Biochem. Biophys. Res. Commun., 264(3), 921-8.
    • (1999) Biochem. Biophys. Res. Commun. , vol.264 , Issue.3 , pp. 921-928
    • Kassner, P.D.1    Burg, M.A.2    Baird, A.3    Larocca, D.4
  • 133
    • 28444488346 scopus 로고    scopus 로고
    • Filamentous phage display in the new millennium
    • Kehoe, J. W., & Kay, B. K. (2005). Filamentous phage display in the new millennium. Chem. Rev., 105(11), 4056-72.
    • (2005) Chem. Rev. , vol.105 , Issue.11 , pp. 4056-4072
    • Kehoe, J.W.1    Kay, B.K.2
  • 134
    • 4344679634 scopus 로고    scopus 로고
    • Detection of invasive colon cancer using a novel, targeted, library-derived fluorescent peptide
    • Kelly, K., Alencar, H., Funovics, M., Mahmood, U., & Weissleder, R. (2004). Detection of invasive colon cancer using a novel, targeted, library-derived fluorescent peptide. Cancer Res., 64 (17), 6247-51.
    • (2004) Cancer Res. , vol.64 , Issue.17 , pp. 6247-6251
    • Kelly, K.1    Alencar, H.2    Funovics, M.3    Mahmood, U.4    Weissleder, R.5
  • 135
    • 33646247173 scopus 로고    scopus 로고
    • High-throughput identification of phage-derived imaging agents
    • Kelly, K. A., Clemons, P. A., Yu, A. M., & Weissleder, R. (2006). High-throughput identification of phage-derived imaging agents. Mol. Imaging, 5(1), 24-30.
    • (2006) Mol. Imaging , vol.5 , Issue.1 , pp. 24-30
    • Kelly, K.A.1    Clemons, P.A.2    Yu, A.M.3    Weissleder, R.4
  • 136
    • 33845564339 scopus 로고    scopus 로고
    • In vivo imaging of molecularly targeted phage
    • Kelly, K. A., Waterman, P., & Weissleder, R. (2006). In vivo imaging of molecularly targeted phage. Neoplasia, 8(12), 1011-8.
    • (2006) Neoplasia , vol.8 , Issue.12 , pp. 1011-1018
    • Kelly, K.A.1    Waterman, P.2    Weissleder, R.3
  • 138
    • 0034635335 scopus 로고    scopus 로고
    • Fully synthetic human combinatorial antibody libraries (HuCAL) based on modular consensus frameworks and CDRs randomized with trinucleotides
    • Knappik, A., Ge, L., Honegger, A., Pack, P., Fischer, M., Wellnhofer, G., Hoess, A., Wolle, J., Plückthun, A., & Virnekas, B. (2000). Fully synthetic human combinatorial antibody libraries (HuCAL) based on modular consensus frameworks and CDRs randomized with trinucleotides. J. Mol. Biol., 296, 57-86.
    • (2000) J. Mol. Biol. , vol.296 , pp. 57-86
    • Knappik, A.1    Ge, L.2    Honegger, A.3    Pack, P.4    Fischer, M.5    Wellnhofer, G.6    Hoess, A.7    Wolle, J.8    Plückthun, A.9    Virnekas, B.10
  • 140
    • 0032509129 scopus 로고    scopus 로고
    • The fibronectin type III domain as a scaffold for novel binding proteins
    • Koide, A., Bailey, C. W., Huang, X., & Koide, S. (1998). The fibronectin type III domain as a scaffold for novel binding proteins. J. Mol. Biol., 284, 1141-51.
    • (1998) J. Mol. Biol. , vol.284 , pp. 1141-1151
    • Koide, A.1    Bailey, C.W.2    Huang, X.3    Koide, S.4
  • 141
    • 0032141295 scopus 로고    scopus 로고
    • Polypyrrole as a model membrane for drug delivery
    • Konturri, K., Pentti, P., & Sundholm, G. (1998). Polypyrrole as a model membrane for drug delivery. J. Electroanal. Chem., 453, 231-8.
    • (1998) J. Electroanal. Chem. , vol.453 , pp. 231-238
    • Konturri, K.1    Pentti, P.2    Sundholm, G.3
  • 142
    • 0035161266 scopus 로고    scopus 로고
    • Identifying diagnostic peptides for lyme disease through epitope discovery
    • Kouzmitcheva, G. A., Petrenko, V. A., & Smith, G. P. (2001). Identifying diagnostic peptides for lyme disease through epitope discovery. Clin. Diagn. Lab. Immunol., 8, 150-60.
    • (2001) Clin. Diagn. Lab. Immunol. , vol.8 , pp. 150-160
    • Kouzmitcheva, G.A.1    Petrenko, V.A.2    Smith, G.P.3
  • 145
    • 0031759422 scopus 로고    scopus 로고
    • Proteolytic selection for protein folding using filamentous bacteriophages
    • Kristensen, P., & Winter, G. (1998). Proteolytic selection for protein folding using filamentous bacteriophages. Fold. Des., 3, 321-8.
    • (1998) Fold. Des. , vol.3 , pp. 321-328
    • Kristensen, P.1    Winter, G.2
  • 146
    • 0028839787 scopus 로고
    • Constrained peptides as binding entities
    • Ladner, R. C. (1995). Constrained peptides as binding entities. Trends Biotechnol., 13, 426-30.
    • (1995) Trends Biotechnol. , vol.13 , pp. 426-430
    • Ladner, R.C.1
  • 147
    • 2942560767 scopus 로고    scopus 로고
    • Phage display-derived peptides as therapeutic alternatives to antibodies
    • Ladner, R. C., Sato, A. K., Gorzelany, J., & de Souza, M. (2004). Phage display-derived peptides as therapeutic alternatives to antibodies. Drug Discov. Today, 9, 525-9.
    • (2004) Drug Discov. Today , vol.9 , pp. 525-529
    • Ladner, R.C.1    Sato, A.K.2    Gorzelany, J.3    de Souza, M.4
  • 149
    • 1842484779 scopus 로고    scopus 로고
    • Designing materials for biology and medicine
    • Langer, R., & Tirrell, D. A. (2004). Designing materials for biology and medicine. Nature, 428, 487-92.
    • (2004) Nature , vol.428 , pp. 487-492
    • Langer, R.1    Tirrell, D.A.2
  • 150
    • 0032921983 scopus 로고    scopus 로고
    • Gene transfer to mammalian cells using genetically targeted filamentous bacteriophage
    • Larocca, D., Kassner, P. D., Witte, A., Ladnera, R. C., Pierce, G. F., & Baird, A. (1999). Gene transfer to mammalian cells using genetically targeted filamentous bacteriophage. FASEB J., 13, 727-34.
    • (1999) FASEB J. , vol.13 , pp. 727-734
    • Larocca, D.1    Kassner, P.D.2    Witte, A.3    Ladnera, R.C.4    Pierce, G.F.5    Baird, A.6
  • 151
    • 0032211231 scopus 로고    scopus 로고
    • Targeting bacteriophage to mammalian cell surface receptors for gene delivery
    • Larocca, D., Witte, A., Johnson, W., Pierce, G. F., & Baird, A. (1998). Targeting bacteriophage to mammalian cell surface receptors for gene delivery. Hum. Gene Ther., 9, 2393-9.
    • (1998) Hum. Gene Ther. , vol.9 , pp. 2393-2399
    • Larocca, D.1    Witte, A.2    Johnson, W.3    Pierce, G.F.4    Baird, A.5
  • 153
    • 0036674043 scopus 로고    scopus 로고
    • Identification of synovium-specific homing peptides by in vivo phage display selection
    • Lee, L.., Buckley, C., Blades, M. C., Panayi, G., George, A. J., & Pitzalis, C. (2002). Identification of synovium-specific homing peptides by in vivo phage display selection. Arthritis Rheum., 48(8), 2109-20.
    • (2002) Arthritis Rheum. , vol.48 , Issue.8 , pp. 2109-2120
    • Lee, L.1    Buckley, C.2    Blades, M.C.3    Panayi, G.4    George, A.J.5    Pitzalis, C.6
  • 154
    • 0037012921 scopus 로고    scopus 로고
    • Ordering of quantum dots using genetically engineered viruses
    • Lee, S.-W., Mao, C., Flynn, C. E., & Belcher, A. M. (2002). Ordering of quantum dots using genetically engineered viruses. Science, 296, 892-5.
    • (2002) Science , vol.296 , pp. 892-895
    • Lee, S.-W.1    Mao, C.2    Flynn, C.E.3    Belcher, A.M.4
  • 155
    • 0037094362 scopus 로고    scopus 로고
    • Construction and exploitation in model experiments of functional selection of a landscape library expressed from a phagemid
    • Legendre, D., & Fastrez, J. (2002). Construction and exploitation in model experiments of functional selection of a landscape library expressed from a phagemid. Gene, 290, 203-15.
    • (2002) Gene , vol.290 , pp. 203-215
    • Legendre, D.1    Fastrez, J.2
  • 156
    • 0036892257 scopus 로고    scopus 로고
    • Epitope mapping of antibodies against prostate-specific antigen with use of peptide libraries
    • Leinonen, J., Wu, P., & Stenman, U. H. (2002). Epitope mapping of antibodies against prostate-specific antigen with use of peptide libraries. Clin. Chem., 48, 2208-16.
    • (2002) Clin. Chem. , vol.48 , pp. 2208-2216
    • Leinonen, J.1    Wu, P.2    Stenman, U.H.3
  • 157
    • 33747467583 scopus 로고    scopus 로고
    • Molecular addresses of tumors: selection by in vivo phage display
    • Li, X. B., Schluesener, H. J., & Xu, S. Q. (2006). Molecular addresses of tumors: selection by in vivo phage display. Arch. Immunol. Ther. Exp. (Warsz), 54(3), 177-81.
    • (2006) Arch. Immunol. Ther. Exp. (Warsz) , vol.54 , Issue.3 , pp. 177-181
    • Li, X.B.1    Schluesener, H.J.2    Xu, S.Q.3
  • 158
    • 33747467583 scopus 로고    scopus 로고
    • Molecular addresses of tumors: selection by in vivo phage display
    • Li, X. B., Schluesener, H. J., & Xu, S. Q. (2006). Molecular addresses of tumors: selection by in vivo phage display. Arch. Immunol. Ther. Exp. (Warsz), 54(3), 177-81.
    • (2006) Arch. Immunol. Ther. Exp. (Warsz) , vol.54 , Issue.3 , pp. 177-181
    • Li, X.B.1    Schluesener, H.J.2    Xu, S.Q.3
  • 159
    • 34047192439 scopus 로고    scopus 로고
    • Cell-targeted phagemid particles preparation using Escherichia coli bearing ligand-pIII encoding helper phage genome
    • Li, Z., Jiang, H., Zhan, J., & Gu J. (2006). Cell-targeted phagemid particles preparation using Escherichia coli bearing ligand-pIII encoding helper phage genome. Biotechniques, 41(6), 706-7.
    • (2006) Biotechniques , vol.41 , Issue.6 , pp. 706-707
    • Li, Z.1    Jiang, H.2    Zhan, J.3    Gu, J.4
  • 160
    • 32944466915 scopus 로고    scopus 로고
    • Preparation of peptide-targeted phagemid particles using a protein III-modified helper phage
    • Li, Z., Zhang, J., Zhao, R., Xu, Y., & Gu, J. (2005). Preparation of peptide-targeted phagemid particles using a protein III-modified helper phage. Biotechniques, 39(4), 493-97.
    • (2005) Biotechniques , vol.39 , Issue.4 , pp. 493-497
    • Li, Z.1    Zhang, J.2    Zhao, R.3    Xu, Y.4    Gu, J.5
  • 162
    • 3142685154 scopus 로고    scopus 로고
    • In-vitro protein evolution by ribosome display and mRNA display
    • Lipovsek, D., & Plückthun, A. (2004). In-vitro protein evolution by ribosome display and mRNA display. J. Imm. Methods, 290, 51-67.
    • (2004) J. Imm. Methods , vol.290 , pp. 51-67
    • Lipovsek, D.1    Plückthun, A.2
  • 163
    • 0034327783 scopus 로고    scopus 로고
    • Applying phage antibodies to proteomics: selecting single chain Fv antibodies to antigens blotted on nitrocellulose
    • Liu, B., & Marks, J. D. (2000). Applying phage antibodies to proteomics: selecting single chain Fv antibodies to antigens blotted on nitrocellulose. Anal. Biochem., 286, 119-28.
    • (2000) Anal. Biochem. , vol.286 , pp. 119-128
    • Liu, B.1    Marks, J.D.2
  • 164
    • 58249134906 scopus 로고    scopus 로고
    • Phage-displayed protein chip based on SPR sensing
    • Sens. Actuators B: Chem., doi:10.1016/j.snb.2008.11.031
    • Liu, F., Luo, Z., Ding, X., Zhu, S. & Yu, X. (2008). Phage-displayed protein chip based on SPR sensing. Sens. Actuators B: Chem., doi:10.1016/j.snb.2008.11.031.
    • (2008)
    • Liu, F.1    Luo, Z.2    Ding, X.3    Zhu, S.4    Yu, X.5
  • 166
    • 34547952070 scopus 로고    scopus 로고
    • In vivo selection and validation of liver-specific ligands using a new T7 phage peptide display system
    • Ludtke, J. J., Sololoff, A. V., Wong, S. C., Zhang, G., & Wolff, J. A. (2007). In vivo selection and validation of liver-specific ligands using a new T7 phage peptide display system. Drug Deliv., 14(6), 357-69.
    • (2007) Drug Deliv. , vol.14 , Issue.6 , pp. 357-369
    • Ludtke, J.J.1    Sololoff, A.V.2    Wong, S.C.3    Zhang, G.4    Wolff, J.A.5
  • 167
    • 34249694964 scopus 로고    scopus 로고
    • Chemical aspects of synthetic biology
    • Luisi, P. L. (2007). Chemical aspects of synthetic biology. Chemistry and Biodiversity, 4, 603-21.
    • (2007) Chemistry and Biodiversity , vol.4 , pp. 603-621
    • Luisi, P.L.1
  • 169
    • 24744448249 scopus 로고    scopus 로고
    • Peptide inhibitor of pancreatic lipase selected by phage display using different elution strategies
    • Lunder, M., Bratkovic, T., Kreft, S., & Strukelj, B. (2005b). Peptide inhibitor of pancreatic lipase selected by phage display using different elution strategies. J. Lipid Res., 46(7), 1512-6.
    • (2005) J. Lipid Res. , vol.46 , Issue.7 , pp. 1512-1516
    • Lunder, M.1    Bratkovic, T.2    Kreft, S.3    Strukelj, B.4
  • 170
    • 0031607130 scopus 로고    scopus 로고
    • Construction of disulfide-constrained random peptide libraries displayed on phage coat protein VIII
    • Luzzago, A., & Felici, F. (1998). Construction of disulfide-constrained random peptide libraries displayed on phage coat protein VIII. Methods Mol. Biol., 87, 155-64.
    • (1998) Methods Mol. Biol. , vol.87 , pp. 155-164
    • Luzzago, A.1    Felici, F.2
  • 173
    • 1842427377 scopus 로고    scopus 로고
    • Genetic immunization against hepatitis B using whole bacteriophage lambda particles
    • March, J. B., Clark, J. R., & Jepson, C. D. (2004). Genetic immunization against hepatitis B using whole bacteriophage lambda particles. Vaccine, 22, 1666-71.
    • (2004) Vaccine , vol.22 , pp. 1666-1671
    • March, J.B.1    Clark, J.R.2    Jepson, C.D.3
  • 175
    • 0032054113 scopus 로고    scopus 로고
    • Filamentous phage structure, infection and assembly
    • Marvin, D.A. (1998). Filamentous phage structure, infection and assembly. Curr. Opin. Struct. Biol., 8, 150-8.
    • (1998) Curr. Opin. Struct. Biol. , vol.8 , pp. 150-158
    • Marvin, D.A.1
  • 176
    • 0028592703 scopus 로고
    • An in vitro polysome display system for identifying ligands from very large peptide libraries
    • Mattheakis, L. C., Bhatt, R. R., & Dower, W.J. (1994). An in vitro polysome display system for identifying ligands from very large peptide libraries. Proc. Natl. Acad. Sci. USA, 91, 9022-6.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 9022-9026
    • Mattheakis, L.C.1    Bhatt, R.R.2    Dower, W.J.3
  • 177
    • 0038498064 scopus 로고    scopus 로고
    • Engineering exosite peptides for complete inhibition of factor VIIa using a protease switch with substrate phage
    • Maun, H. R., Eigenbrot, C., & Lazarus, R. A. (2003). Engineering exosite peptides for complete inhibition of factor VIIa using a protease switch with substrate phage. J. Biol. Chem., 278, 21823-30.
    • (2003) J. Biol. Chem. , vol.278 , pp. 21823-21830
    • Maun, H.R.1    Eigenbrot, C.2    Lazarus, R.A.3
  • 178
    • 0025226085 scopus 로고
    • Phage antibodies: filamentous phage displaying antibody variable domains
    • McCafferty, J., Griffiths, A. D., Winter, G., & Chiswell, D. J. (1990). Phage antibodies: filamentous phage displaying antibody variable domains. Nature, 348, 552-4.
    • (1990) Nature , vol.348 , pp. 552-554
    • McCafferty, J.1    Griffiths, A.D.2    Winter, G.3    Chiswell, D.J.4
  • 180
    • 0001367290 scopus 로고
    • Genetically directed synthesis of new polymeric materials. Expression of artificial genes encoding proteins with repeating-(AlaGly)3ProGluGly-elements
    • McGrath, K. P., Fournier, M. J., Mason, T. L., & Tirrell, D. A. (1992). Genetically directed synthesis of new polymeric materials. Expression of artificial genes encoding proteins with repeating-(AlaGly)3ProGluGly-elements. J. Am. Chem. Soc., 114, 727-33.
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 727-733
    • McGrath, K.P.1    Fournier, M.J.2    Mason, T.L.3    Tirrell, D.A.4
  • 182
    • 0027253452 scopus 로고
    • M13 bacteriophage displaying disulfide-constrained microproteins
    • McLafferty, M. A., Kent, R. B., Ladner, R. C., & Markland, W. (1993). M13 bacteriophage displaying disulfide-constrained microproteins. Gene, 128, 29-36.
    • (1993) Gene , vol.128 , pp. 29-36
    • McLafferty, M.A.1    Kent, R.B.2    Ladner, R.C.3    Markland, W.4
  • 183
    • 0028917153 scopus 로고
    • Derivation of vaccines from mimotopes. Immunologic properties of human hepatitis B virus surface antigen mimotopes displayed on filamentous phage
    • Meola, A., Delmastro, P., Monaci, P., Luzzago, A., Nicosia, A., Felici, F., Cortese, R., & Galfre, G. (1995). Derivation of vaccines from mimotopes. Immunologic properties of human hepatitis B virus surface antigen mimotopes displayed on filamentous phage. J. Immunol., 154, 3162-72.
    • (1995) J. Immunol. , vol.154 , pp. 3162-3172
    • Meola, A.1    Delmastro, P.2    Monaci, P.3    Luzzago, A.4    Nicosia, A.5    Felici, F.6    Cortese, R.7    Galfre, G.8
  • 184
    • 0027241243 scopus 로고
    • Design of specific immunogens using filamentous phage as the carrier
    • Minenkova, O. O., Ilyichev, A. A., Kishchenko, G. P., & Petrenko, V. A. (1993). Design of specific immunogens using filamentous phage as the carrier. Gene, 128, 85-88.
    • (1993) Gene , vol.128 , pp. 85-88
    • Minenkova, O.O.1    Ilyichev, A.A.2    Kishchenko, G.P.3    Petrenko, V.A.4
  • 185
    • 0036346217 scopus 로고    scopus 로고
    • Uptake and processing of modified bacteriophage M13 in mice: implications for phage display
    • Molenaar, T. J., Michon, I., de Haas, S. A. M., van Berkel, T. J. C., Kuiper, J., & Biessen, E. A. L. (2002). Uptake and processing of modified bacteriophage M13 in mice: implications for phage display. Virology, 293, 182-91.
    • (2002) Virology , vol.293 , pp. 182-191
    • Molenaar, T.J.1    Michon, I.2    de Haas, S.A.M.3    van Berkel, T.J.C.4    Kuiper, J.5    Biessen, E.A.L.6
  • 188
    • 0034292407 scopus 로고    scopus 로고
    • Conformational epitopes on the diabetes autoantigen GAD65 identified by peptide phage display and molecular modelling
    • Myers, M. A., Davies, J. M., Tong, J. C., Whisstock, J., Scealy, M., Mackay, I. R., & Rowley, M. J. (2000). Conformational epitopes on the diabetes autoantigen GAD65 identified by peptide phage display and molecular modelling. J. Immunol., 165, 3830-8.
    • (2000) J. Immunol. , vol.165 , pp. 3830-3838
    • Myers, M.A.1    Davies, J.M.2    Tong, J.C.3    Whisstock, J.4    Scealy, M.5    Mackay, I.R.6    Rowley, M.J.7
  • 190
    • 0035928727 scopus 로고    scopus 로고
    • A novel family of hairpin peptides that inhibit IgE activity by binding to the high-affinity IgE receptor
    • Nakamura, G. R., Starovasnik, M. A., Reynolds, M. E., & Lowman, H. B. (2001). A novel family of hairpin peptides that inhibit IgE activity by binding to the high-affinity IgE receptor. Biochemistry, 40, 9828-35.
    • (2001) Biochemistry , vol.40 , pp. 9828-9835
    • Nakamura, G.R.1    Starovasnik, M.A.2    Reynolds, M.E.3    Lowman, H.B.4
  • 192
    • 0842287344 scopus 로고    scopus 로고
    • Genetically driven assembly of nanorings based on the M13 virus
    • Nam, K. T., Peelle, B. R., Lee, S.-W., & Belcher, A. M. (2004). Genetically driven assembly of nanorings based on the M13 virus. Nano Lett., 4, 23-7.
    • (2004) Nano Lett. , vol.4 , pp. 23-27
    • Nam, K.T.1    Peelle, B.R.2    Lee, S.-W.3    Belcher, A.M.4
  • 194
    • 34548583912 scopus 로고    scopus 로고
    • SPR biosensor for the detection of L. monocytogenes using phage-displayed antibody
    • Nanduri, V., Bhunia, A. K., Tu, S.-I., Paoli, G. C., & Brewster, J. D. (2007b). SPR biosensor for the detection of L. monocytogenes using phage-displayed antibody. Biosens. Bioelectr., 23, 248-52.
    • (2007) Biosens. Bioelectr. , vol.23 , pp. 248-252
    • Nanduri, V.1    Bhunia, A.K.2    Tu, S.-I.3    Paoli, G.C.4    Brewster, J.D.5
  • 196
    • 0031559943 scopus 로고    scopus 로고
    • In vitro virus: bonding of mRNA bearing puromycin at the 3′-terminal end to the C-terminal end of its encoded protein on the ribosome in vitro
    • Nemoto, N., Miyamoto-Sato, E., Husimi, Y., & Yanagawa, H. (1997). In vitro virus: bonding of mRNA bearing puromycin at the 3′-terminal end to the C-terminal end of its encoded protein on the ribosome in vitro. FEBS Lett., 414, 405-8.
    • (1997) FEBS Lett. , vol.414 , pp. 405-408
    • Nemoto, N.1    Miyamoto-Sato, E.2    Husimi, Y.3    Yanagawa, H.4
  • 197
    • 33749042410 scopus 로고    scopus 로고
    • In vivo selection of phage for the optical imaging of PC-3 human prostate carcinoma in mice
    • Newton, J. R., Kelly, K. A., Mahmood, U., Weissleder, R., & Deutscher, S. L. (2006). In vivo selection of phage for the optical imaging of PC-3 human prostate carcinoma in mice. Neoplasia, 8(9), 772-80.
    • (2006) Neoplasia , vol.8 , Issue.9 , pp. 772-780
    • Newton, J.R.1    Kelly, K.A.2    Mahmood, U.3    Weissleder, R.4    Deutscher, S.L.5
  • 198
    • 34247205399 scopus 로고    scopus 로고
    • Melanoma imaging with pretargeted bivalent bacteriophage
    • Newton, J. R., Miao, Y., Deutscher, S. L., & Quinn, T. P. (2007). Melanoma imaging with pretargeted bivalent bacteriophage. J. Nucl. Med. 48 (3), 429-36.
    • (2007) J. Nucl. Med. , vol.48 , Issue.3 , pp. 429-436
    • Newton, J.R.1    Miao, Y.2    Deutscher, S.L.3    Quinn, T.P.4
  • 199
    • 52049124013 scopus 로고    scopus 로고
    • Coupling methods to obtain ligand-targeted liposomes and nanoparticles
    • Nobs, L., Buchegger, F., Gurny, R., & Allemann, E. (2006). Coupling methods to obtain ligand-targeted liposomes and nanoparticles. Drugs Pharm. Sci., 158, 123-148.
    • (2006) Drugs Pharm. Sci. , vol.158 , pp. 123-148
    • Nobs, L.1    Buchegger, F.2    Gurny, R.3    Allemann, E.4
  • 200
    • 0029981792 scopus 로고    scopus 로고
    • Light chain shuffling of a high affinity antibody results in a drift in epitope recognition
    • Ohlin, M., Owman, H., Mach, M., & Borrebaeck, C. A. (1996). Light chain shuffling of a high affinity antibody results in a drift in epitope recognition. Mol. Immunol., 33, 47-56.
    • (1996) Mol. Immunol. , vol.33 , pp. 47-56
    • Ohlin, M.1    Owman, H.2    Mach, M.3    Borrebaeck, C.A.4
  • 201
    • 31044438679 scopus 로고    scopus 로고
    • Affinity-selected filamentous bacteriophage as a probe for acoustic wave biodetectors of Salmonella typhimurium
    • Olsen, E. V., Sorokulova, I. B., Petrenko, V. A., Chen, I. H., Barbaree, J. M., & Vodyanoy, V. J. (2006). Affinity-selected filamentous bacteriophage as a probe for acoustic wave biodetectors of Salmonella typhimurium. Biosens. Bioelectron., 21(8), 1434-42.
    • (2006) Biosens. Bioelectron. , vol.21 , Issue.8 , pp. 1434-1442
    • Olsen, E.V.1    Sorokulova, I.B.2    Petrenko, V.A.3    Chen, I.H.4    Barbaree, J.M.5    Vodyanoy, V.J.6
  • 204
    • 1542698957 scopus 로고
    • Cloning immunoglobulin variable domains for expression by the polymerase chain reaction
    • Orlandi, R., Güssow, D. H., Jones, P. T., & Winter, G. (1989). Cloning immunoglobulin variable domains for expression by the polymerase chain reaction. Proc. Natl. Acad. Sci. USA, 86, 3833-7.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 3833-3837
    • Orlandi, R.1    Güssow, D.H.2    Jones, P.T.3    Winter, G.4
  • 205
    • 0029932458 scopus 로고    scopus 로고
    • Organ targeting in vivo using phage display peptide libraries
    • Pasqualini, R,. & Ruoslahti, E. (1996). Organ targeting in vivo using phage display peptide libraries. Nature, 380(6572), 364-6.
    • (1996) Nature , vol.380 , Issue.6572 , pp. 364-366
    • Pasqualini, R.1    Ruoslahti, E.2
  • 206
    • 0026057989 scopus 로고
    • Generation of diverse high-affinity human monoclonal antibodies by repertoire cloning
    • Persson, M.A., Caothien, R. H., & Burton, D. R. (1991). Generation of diverse high-affinity human monoclonal antibodies by repertoire cloning. Proc. Natl. Acad. Sci. USA, 88, 2432-6.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 2432-2436
    • Persson, M.A.1    Caothien, R.H.2    Burton, D.R.3
  • 207
    • 0242666372 scopus 로고    scopus 로고
    • Mapping of a conformational epitope shared between E1 and E2 on the serum-derived human hepatitis C virus envelope
    • Petit, M. A., Jolivet-Reynaud, C., Peronnet, E., Michal, Y., & Trepo, C. (2003). Mapping of a conformational epitope shared between E1 and E2 on the serum-derived human hepatitis C virus envelope. J. Biol. Chem., 278, 44385-92.
    • (2003) J. Biol. Chem. , vol.278 , pp. 44385-44392
    • Petit, M.A.1    Jolivet-Reynaud, C.2    Peronnet, E.3    Michal, Y.4    Trepo, C.5
  • 208
    • 52049117189 scopus 로고    scopus 로고
    • Evolution of phage display: from bioactive peptides to bioselective nanomaterials
    • Petrenko, V. A. (2008a). Evolution of phage display: from bioactive peptides to bioselective nanomaterials. Review. Expert Opin. Drug Deliv., 5(8), 1-12.
    • (2008) Review. Expert Opin. Drug Deliv. , vol.5 , Issue.8 , pp. 1-12
    • Petrenko, V.A.1
  • 209
    • 38749121322 scopus 로고    scopus 로고
    • Landscape phage as a molecular recognition interface for detection devices
    • Petrenko, V. A. (2008b). Landscape phage as a molecular recognition interface for detection devices. Microelectron. J., 39(2), 202-7.
    • (2008) Microelectron. J. , vol.39 , Issue.2 , pp. 202-207
    • Petrenko, V.A.1
  • 210
    • 0033829057 scopus 로고    scopus 로고
    • Phages from landscape libraries as substitute antibodies
    • Petrenko, V. A., & Smith, G. P. (2000). Phages from landscape libraries as substitute antibodies. Protein. Eng., 13, 589-92.
    • (2000) Protein. Eng. , vol.13 , pp. 589-592
    • Petrenko, V.A.1    Smith, G.P.2
  • 211
    • 3242709714 scopus 로고    scopus 로고
    • Detection of biological threats. A challenge for directed molecular evolution
    • Petrenko, V. A., & Sorokulova, I. B. (2004). Detection of biological threats. A challenge for directed molecular evolution. J. Microbiol. Methods, 58, 147-68.
    • (2004) J. Microbiol. Methods , vol.58 , pp. 147-168
    • Petrenko, V.A.1    Sorokulova, I.B.2
  • 212
    • 0037401049 scopus 로고    scopus 로고
    • Phage display for detection of biological threat agents
    • Petrenko, V. A., & Vodyanoy, V. J. (2003). Phage display for detection of biological threat agents. J. Microbiol. Methods, 53, 253-62.
    • (2003) J. Microbiol. Methods , vol.53 , pp. 253-262
    • Petrenko, V.A.1    Vodyanoy, V.J.2
  • 213
    • 0029793463 scopus 로고    scopus 로고
    • A library of organic landscapes on filamentous phage
    • Petrenko, V. A., Smith, G. P., Gong, X., & Quinn, T. (1996). A library of organic landscapes on filamentous phage. Protein. Eng., 9, 797-801.
    • (1996) Protein. Eng. , vol.9 , pp. 797-801
    • Petrenko, V.A.1    Smith, G.P.2    Gong, X.3    Quinn, T.4
  • 215
    • 0035833983 scopus 로고    scopus 로고
    • Peptide-derived antagonists of the urokinase receptor. Affinity maturation by combinatorial chemistry, identification of functional epitopes, and inhibitory effect on cancer cell intravasation
    • Ploug, M., Østergaard, S., Gårdsvoll, H., Kovalski, K., Holst-Hansen, C., Holm, A., Ossowski, L., & Danø, K. (2001). Peptide-derived antagonists of the urokinase receptor. Affinity maturation by combinatorial chemistry, identification of functional epitopes, and inhibitory effect on cancer cell intravasation. Biochemistry, 40(40), 12157-68.
    • (2001) Biochemistry , vol.40 , Issue.40 , pp. 12157-12168
    • Ploug, M.1    Ostergaard, S.2    Gårdsvoll, H.3    Kovalski, K.4    Holst-Hansen, C.5    Holm, A.6    Ossowski, L.7    Danø, K.8
  • 216
    • 0033617248 scopus 로고    scopus 로고
    • Targeted gene delivery to mammalian cells by filamentous bacteriophage
    • Poul, M. A., & Marks, J. D. (1999). Targeted gene delivery to mammalian cells by filamentous bacteriophage. J. Mol. Biol., 288 (2), 203-11.
    • (1999) J. Mol. Biol. , vol.288 , Issue.2 , pp. 203-211
    • Poul, M.A.1    Marks, J.D.2
  • 217
    • 0344813702 scopus 로고    scopus 로고
    • Antibody scFv fragments without disulfide bonds made by molecular evolution
    • Proba, K., Wörn, A., Honegger, A., & Plückthun, A. (1998). Antibody scFv fragments without disulfide bonds made by molecular evolution. J. Mol. Biol., 275, 245-53.
    • (1998) J. Mol. Biol. , vol.275 , pp. 245-253
    • Proba, K.1    Wörn, A.2    Honegger, A.3    Plückthun, A.4
  • 218
    • 0030752337 scopus 로고    scopus 로고
    • Phage display of combinatorial antibody libraries
    • Rader, C., & Barbas, C. F. (1997). Phage display of combinatorial antibody libraries. Curr. Opin. Biotechnol., 8, 503-8.
    • (1997) Curr. Opin. Biotechnol. , vol.8 , pp. 503-508
    • Rader, C.1    Barbas, C.F.2
  • 219
  • 220
    • 0032581506 scopus 로고    scopus 로고
    • Phage T4 SOC and HOC display of biologically active, full-length proteins on the viral capsid
    • Ren, Z., & Black, L. W. (1998). Phage T4 SOC and HOC display of biologically active, full-length proteins on the viral capsid. Gene, 215, 439-44.
    • (1998) Gene , vol.215 , pp. 439-444
    • Ren, Z.1    Black, L.W.2
  • 221
    • 0033152942 scopus 로고    scopus 로고
    • Totally in vitro protein selection using mRNA-protein fusions and ribosome display
    • Roberts, R.W. (1999). Totally in vitro protein selection using mRNA-protein fusions and ribosome display. Curr. Opin. Chem. Biol., 3(3), 268-73.
    • (1999) Curr. Opin. Chem. Biol. , vol.3 , Issue.3 , pp. 268-273
    • Roberts, R.W.1
  • 222
    • 0030817279 scopus 로고    scopus 로고
    • RNA-peptide fusions for the in vitro selection of peptides and proteins
    • Roberts, R. W., & Szostak, J. W. (1997). RNA-peptide fusions for the in vitro selection of peptides and proteins. Proc. Natl. Acad. Sci. USA, 94(23), 12297-302.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , Issue.23 , pp. 12297-12302
    • Roberts, R.W.1    Szostak, J.W.2
  • 223
    • 0035371218 scopus 로고    scopus 로고
    • Phage display selection of peptides that affect prostate carcinoma cells attachment and invasion
    • Romanov, V. I., Durand, D. B., & Petrenko, V. A. (2001). Phage display selection of peptides that affect prostate carcinoma cells attachment and invasion. Prostate, 47, 239-51.
    • (2001) Prostate , vol.47 , pp. 239-251
    • Romanov, V.I.1    Durand, D.B.2    Petrenko, V.A.3
  • 225
    • 0034653534 scopus 로고    scopus 로고
    • Prediction of the immunodominant epitope of the pyruvate dehydrogenase complex E2 in primary biliary cirrhosis using phage display
    • Rowley, M. J., Scealy, M., Whisstock, J. C., Jois, J. A., Wijeyewickrema, L. C., & Mackay, I. R. (2000). Prediction of the immunodominant epitope of the pyruvate dehydrogenase complex E2 in primary biliary cirrhosis using phage display. J. Immunol., 164, 3413-9.
    • (2000) J. Immunol. , vol.164 , pp. 3413-3419
    • Rowley, M.J.1    Scealy, M.2    Whisstock, J.C.3    Jois, J.A.4    Wijeyewickrema, L.C.5    Mackay, I.R.6
  • 226
    • 0027247924 scopus 로고
    • Biotin binders selected from a random peptide library expressed on phage
    • Saggio, I. & Laufer, R. (1993). Biotin binders selected from a random peptide library expressed on phage. Biochem. J., 293(3), 613-6.
    • (1993) Biochem. J. , vol.293 , Issue.3 , pp. 613-616
    • Saggio, I.1    Laufer, R.2
  • 228
    • 20144363075 scopus 로고    scopus 로고
    • Biomaterials functionalization using a novel peptide that selectively binds to a conducting polymer
    • Sanghvi, A. B., Miller, K. P.-H., Belcher, A. M., & Schmidt, C. E. (2005). Biomaterials functionalization using a novel peptide that selectively binds to a conducting polymer. Nature Materials, 4, 496-502.
    • (2005) Nature Materials , vol.4 , pp. 496-502
    • Sanghvi, A.B.1    Miller, K.P.-H.2    Belcher, A.M.3    Schmidt, C.E.4
  • 229
    • 0344012217 scopus 로고    scopus 로고
    • A hexapeptide motif that electrostatically binds to the surface of titanium
    • Sano, K., & Shiba, K. (2003). A hexapeptide motif that electrostatically binds to the surface of titanium. J. Am. Chem. Soc., 125, 14234-5.
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 14234-14235
    • Sano, K.1    Shiba, K.2
  • 230
    • 0032508462 scopus 로고    scopus 로고
    • Efficient display of an HCV cDNA expression library as C-terminal fusion to the capsid protein D of bacteriophage lambda
    • Santini, C., Brennan, D., Mennuni, C., Hoess, R. H., Nicosia, A., Cortese, R., & Luzzago, A. (1998). Efficient display of an HCV cDNA expression library as C-terminal fusion to the capsid protein D of bacteriophage lambda. J. Mol. Biol., 282, 125-35.
    • (1998) J. Mol. Biol. , vol.282 , pp. 125-135
    • Santini, C.1    Brennan, D.2    Mennuni, C.3    Hoess, R.H.4    Nicosia, A.5    Cortese, R.6    Luzzago, A.7
  • 233
    • 0033987925 scopus 로고    scopus 로고
    • Exploiting recombination in single bacteria to make large phage antibody libraries
    • Sblattero, D., & Bradbury, A. (2000). Exploiting recombination in single bacteria to make large phage antibody libraries. Nat. Biotechnol., 18, 75-80.
    • (2000) Nat. Biotechnol. , vol.18 , pp. 75-80
    • Sblattero, D.1    Bradbury, A.2
  • 234
    • 0033506261 scopus 로고    scopus 로고
    • Ribosome display: an in vitro method for selection and evolution of antibodies from libraries
    • Schaffitzel, C., Hanes, J., Jermutus, L., & Plückthun, A. (1999). Ribosome display: an in vitro method for selection and evolution of antibodies from libraries. J. Immunol. Methods, 231, 119-35.
    • (1999) J. Immunol. Methods , vol.231 , pp. 119-135
    • Schaffitzel, C.1    Hanes, J.2    Jermutus, L.3    Plückthun, A.4
  • 235
    • 0033215240 scopus 로고    scopus 로고
    • Display cloning: functional identification of natural receptors using cDNA-phage display
    • Sche, P. P., McKenzie, K. M., White, J. D., & Austin, D. J. (1999). Display cloning: functional identification of natural receptors using cDNA-phage display. Chem. Biol., 6, 707-16.
    • (1999) Chem. Biol. , vol.6 , pp. 707-716
    • Sche, P.P.1    McKenzie, K.M.2    White, J.D.3    Austin, D.J.4
  • 236
    • 24044543921 scopus 로고    scopus 로고
    • Identification of a functional epitope of the Nogo receptor by a combinatorial approach using ribosome display
    • Schimmele, B., & Plückthun, A. (2005). Identification of a functional epitope of the Nogo receptor by a combinatorial approach using ribosome display. J. Mol. Biol., 352, 229-41.
    • (2005) J. Mol. Biol. , vol.352 , pp. 229-241
    • Schimmele, B.1    Plückthun, A.2
  • 238
    • 15744396333 scopus 로고    scopus 로고
    • Dual-surface modification of the tobacco mosaic virus
    • Schlick, T. L., Ding, Z., Kovacs, E. W., & Francis, M. B. (2005). Dual-surface modification of the tobacco mosaic virus. J. Am. Chem. Soc., 127, 3718-23.
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 3718-3723
    • Schlick, T.L.1    Ding, Z.2    Kovacs, E.W.3    Francis, M.B.4
  • 239
    • 4644275378 scopus 로고    scopus 로고
    • Selection of recombinant phages binding to pathological endothelial and tumor cells of rat glioblastoma by in vivo display
    • Schluesener, H. J., & Xianglin, T. (2004). Selection of recombinant phages binding to pathological endothelial and tumor cells of rat glioblastoma by in vivo display. J. Neurol. Sci., 224(1-2), 77-82.
    • (2004) J. Neurol. Sci. , vol.224 , Issue.1-2 , pp. 77-82
    • Schluesener, H.J.1    Xianglin, T.2
  • 240
    • 0030793289 scopus 로고    scopus 로고
    • Stimulation of neurite outgrowth using an electrically conducting polymer
    • Schmidt, C. E., Shastri, V. R., Vacanti, J. P., & Langer, R. (1997). Stimulation of neurite outgrowth using an electrically conducting polymer. Proc. Natl Acad. Sci. USA, 94, 8948-53.
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 8948-8953
    • Schmidt, C.E.1    Shastri, V.R.2    Vacanti, J.P.3    Langer, R.4
  • 241
    • 0025112794 scopus 로고
    • Searching for peptide ligands with an epitope library
    • Scott, J. K., & Smith, G. P. (1990). Searching for peptide ligands with an epitope library. Science, 249, 386-90.
    • (1990) Science , vol.249 , pp. 386-390
    • Scott, J.K.1    Smith, G.P.2
  • 242
    • 0032981699 scopus 로고    scopus 로고
    • Toward controlling gene expression at will: selection and design of zinc finger domains recognizing each of the 5'-GNN-3' DNA target sequences
    • Segal, D. J., Dreier, B., Beerli, R. R., & Barbas, C. F. III (1999). Toward controlling gene expression at will: selection and design of zinc finger domains recognizing each of the 5'-GNN-3' DNA target sequences. Proc. Natl. Acad. USA, 96, 2758-63.
    • (1999) Proc. Natl. Acad. USA , vol.96 , pp. 2758-2763
    • Segal, D.J.1    Dreier, B.2    Beerli, R.R.3    Barbas III, C.F.4
  • 243
    • 34547174659 scopus 로고    scopus 로고
    • From phage display to magnetophage, a new tool for magnetic resonance molecular imaging
    • Segers, J., Laumonier, C., Burtea, C., Laurent, S., Elst, L. V., & Muller, R. N. (2007). From phage display to magnetophage, a new tool for magnetic resonance molecular imaging. Bioconjug. Chem. 18(4), 1251-8.
    • (2007) Bioconjug. Chem. , vol.18 , Issue.4 , pp. 1251-1258
    • Segers, J.1    Laumonier, C.2    Burtea, C.3    Laurent, S.4    Elst, L.V.5    Muller, R.N.6
  • 244
    • 33751540859 scopus 로고    scopus 로고
    • Display technologies: application for the discovery of drug and gene delivery agents
    • Sergeeva, A., Kolonin, M. G., Molldrem, J. J., Pasqualini, R., & Arap, W. (2006). Display technologies: application for the discovery of drug and gene delivery agents. Adv. Drug Deliv. Rev., 58(15), 1622-54.
    • (2006) Adv. Drug Deliv. Rev. , vol.58 , Issue.15 , pp. 1622-1654
    • Sergeeva, A.1    Kolonin, M.G.2    Molldrem, J.J.3    Pasqualini, R.4    Arap, W.5
  • 246
    • 0036181477 scopus 로고    scopus 로고
    • Recombinant monoclonal antibody technology
    • Siegel, D. L. (2002). Recombinant monoclonal antibody technology. Transfus. Clin. Biol., 9, 15-22.
    • (2002) Transfus. Clin. Biol. , vol.9 , pp. 15-22
    • Siegel, D.L.1
  • 247
    • 0036300793 scopus 로고    scopus 로고
    • Amino acid determinants of beta-hairpin conformation in erythropoeitin receptor agonist peptides derived from a phage display library
    • Skelton, N. J., Russell, S., de Sauvage, F., & Cochran, A. G. (2002). Amino acid determinants of beta-hairpin conformation in erythropoeitin receptor agonist peptides derived from a phage display library. J. Mol. Biol., 316, 1111-25.
    • (2002) J. Mol. Biol. , vol.316 , pp. 1111-1125
    • Skelton, N.J.1    Russell, S.2    de Sauvage, F.3    Cochran, A.G.4
  • 248
    • 0024292736 scopus 로고
    • Assembly of a functional immunoglobulin Fv fragment in Escherichia coli
    • Skerra, A., & Plückthun, A. (1988). Assembly of a functional immunoglobulin Fv fragment in Escherichia coli. Science, 240, 1038-41.
    • (1988) Science , vol.240 , pp. 1038-1041
    • Skerra, A.1    Plückthun, A.2
  • 249
    • 0021818675 scopus 로고
    • Filamentous fusion phage: novel expression vectors that display cloned antigens on the virion surface
    • Smith, G. P. (1985). Filamentous fusion phage: novel expression vectors that display cloned antigens on the virion surface. Science, 228(4705), 1315-7.
    • (1985) Science , vol.228 , Issue.4705 , pp. 1315-1317
    • Smith, G.P.1
  • 250
    • 0007126138 scopus 로고
    • Cloning in fUSE vectors
    • Available from: Prof. G. P. Smith, Division of Biological Sciences, University of Missouri, URL
    • Smith, G. P. (1992). Cloning in fUSE vectors. Available from: Prof. G. P. Smith, Division of Biological Sciences, University of Missouri, URL: http://www.biosci.missouri.edu/smithgp/PhageDisplayWebsite/PhageDisplayWebsiteIndex.html.
    • (1992)
    • Smith, G.P.1
  • 254
    • 0034902628 scopus 로고    scopus 로고
    • Isolation, characterization, and recovery of small peptide phage display epitopes selected against viable malignant glioma cells
    • Spear, M. A., Breakefield, X. O., Beltzer, J., Schuback, D., Weissleder, R., Pardo, F. S., & Ladner, R. (2001). Isolation, characterization, and recovery of small peptide phage display epitopes selected against viable malignant glioma cells. Cancer Gene Ther., 8, 506-11.
    • (2001) Cancer Gene Ther. , vol.8 , pp. 506-511
    • Spear, M.A.1    Breakefield, X.O.2    Beltzer, J.3    Schuback, D.4    Weissleder, R.5    Pardo, F.S.6    Ladner, R.7
  • 255
    • 0037334891 scopus 로고    scopus 로고
    • Identification of the immunodominant protein and other proteins of the Bacillus anthracis exosporium
    • Steichen, C., Chen, P., Kearney, J. F., & Turnbough, C. L. Jr. (2003). Identification of the immunodominant protein and other proteins of the Bacillus anthracis exosporium. J. Bacteriol., 185, 1903-10.
    • (2003) J. Bacteriol. , vol.185 , pp. 1903-1910
    • Steichen, C.1    Chen, P.2    Kearney, J.F.3    Turnbough Jr., C.L.4
  • 256
    • 0028050350 scopus 로고
    • Rapid evolution of a protein in vitro by DNA shuffling
    • Stemmer, W. P. (1994). Rapid evolution of a protein in vitro by DNA shuffling. Nature, 370(6488), 389-91.
    • (1994) Nature , vol.370 , Issue.6488 , pp. 389-391
    • Stemmer, W.P.1
  • 257
    • 34249006601 scopus 로고    scopus 로고
    • Promise and progress for functional and molecular imaging of response to targeted therapies
    • Stephen, R. M., & Gillies, R. J. (2007). Promise and progress for functional and molecular imaging of response to targeted therapies. Pharm. Res. 24(6), 1172-85.
    • (2007) Pharm. Res. , vol.24 , Issue.6 , pp. 1172-1185
    • Stephen, R.M.1    Gillies, R.J.2
  • 258
    • 0036840938 scopus 로고    scopus 로고
    • Development of a peptide-mediated capture PCR for detection of Mycobacterium avium subsp. paratuberculosis in milk
    • Stratmann, J., Strommenger, B., Stevenson, K., & Gerlach, G. F. (2002). Development of a peptide-mediated capture PCR for detection of Mycobacterium avium subsp. paratuberculosis in milk. J. Clin. Microbiol., 40, 4244-50.
    • (2002) J. Clin. Microbiol. , vol.40 , pp. 4244-4250
    • Stratmann, J.1    Strommenger, B.2    Stevenson, K.3    Gerlach, G.F.4
  • 260
    • 0036603896 scopus 로고    scopus 로고
    • In vivo phage display and vascular heterogeneity: implications for targeted medicine
    • Trepel, M., Arap, W., & Pasqualini, R. (2002). In vivo phage display and vascular heterogeneity: implications for targeted medicine. Curr. Opin. Chem. Biol., 6, 399-404.
    • (2002) Curr. Opin. Chem. Biol. , vol.6 , pp. 399-404
    • Trepel, M.1    Arap, W.2    Pasqualini, R.3
  • 261
    • 34247495642 scopus 로고    scopus 로고
    • Digital memory device based on tobacco mosaic virus conjugated with nanoparticles
    • Tseng, R. J., Tsai, C., Ma, L., Ouyang, J., Ozkan, C. S., & Yang, Y. (2006). Digital memory device based on tobacco mosaic virus conjugated with nanoparticles. Nature Nanotechnology, 1, 72-7.
    • (2006) Nature Nanotechnology , vol.1 , pp. 72-77
    • Tseng, R.J.1    Tsai, C.2    Ma, L.3    Ouyang, J.4    Ozkan, C.S.5    Yang, Y.6
  • 262
    • 0037400895 scopus 로고    scopus 로고
    • Discovery of phage display peptide ligands for species-specific detection of Bacillus spores
    • Turnbough, C. L. Jr. (2003). Discovery of phage display peptide ligands for species-specific detection of Bacillus spores. J. Microbiol. Methods, 53, 263-71.
    • (2003) J. Microbiol. Methods , vol.53 , pp. 263-271
    • Turnbough Jr., C.L.1
  • 265
    • 0026501041 scopus 로고
    • Electrically conductive polymeric substrates enhance nerve fibre outgrowth in vitro
    • Valentini, R. F., Vargo, T. G., Gardella, J. A. Jr., & Aebischer, P. (1992). Electrically conductive polymeric substrates enhance nerve fibre outgrowth in vitro. Biomater., 13, 183-90.
    • (1992) Biomater. , vol.13 , pp. 183-190
    • Valentini, R.F.1    Vargo, T.G.2    Gardella Jr., J.A.3    Aebischer, P.4
  • 266
    • 0029584350 scopus 로고
    • Identification of functional interaction sites on proteins using bacteriophage-displayed random epitope libraries
    • van Zonneveld, A. J., van den Berg, B. M. M., van Meijer, M., & Pannekoek, H. (1995). Identification of functional interaction sites on proteins using bacteriophage-displayed random epitope libraries. Gene, 167, 49-52.
    • (1995) Gene , vol.167 , pp. 49-52
    • van Zonneveld, A.J.1    van den Berg, B.M.M.2    van Meijer, M.3    Pannekoek, H.4
  • 267
    • 0032999633 scopus 로고    scopus 로고
    • In situ preparation of a cholesterol biosensor: entrapment of cholesterol oxidase in an overoxidized polypyrrole film electrodeposited in a flow system: Determination of total cholesterol in serum
    • Vidal, J. C., Garcia, E., & Castillo, J. R. (1999). In situ preparation of a cholesterol biosensor: entrapment of cholesterol oxidase in an overoxidized polypyrrole film electrodeposited in a flow system: Determination of total cholesterol in serum. Anal. Chim. Acta., 385, 213-22.
    • (1999) Anal. Chim. Acta. , vol.385 , pp. 213-222
    • Vidal, J.C.1    Garcia, E.2    Castillo, J.R.3
  • 268
    • 33745727452 scopus 로고    scopus 로고
    • Highly efficient ribosome display selection by use of purified components for in vitro translation
    • Villemagne, D., Jackson, R., & Douthwaite, J. A. (2006). Highly efficient ribosome display selection by use of purified components for in vitro translation. J. Immunol. Methods, 313, 140-8.
    • (2006) J. Immunol. Methods , vol.313 , pp. 140-148
    • Villemagne, D.1    Jackson, R.2    Douthwaite, J.A.3
  • 269
    • 35348960484 scopus 로고    scopus 로고
    • Detection of Bacillus anthracis spores in liquid using phage-based magnetoelastic micro-resonators
    • Wan, J., Johnson, M. L., Guntupalli, R., Petrenko, V. A., & Chin, B. A. (2007a). Detection of Bacillus anthracis spores in liquid using phage-based magnetoelastic micro-resonators. Sensors Actuators B, 127, 559-66.
    • (2007) Sensors Actuators B , vol.127 , pp. 559-566
    • Wan, J.1    Johnson, M.L.2    Guntupalli, R.3    Petrenko, V.A.4    Chin, B.A.5
  • 270
    • 85008008212 scopus 로고    scopus 로고
    • Phage-based magnetoelastic wireless biosensors for detecting Bacillus anthracis spores
    • Wan, J., Shu, H., Huang, S., Fiebor, B., Chen, I. H., Petrenko, V. A., & Chin, B. A. (2007b). Phage-based magnetoelastic wireless biosensors for detecting Bacillus anthracis spores. IEEE Sensors J., 7(3), 470-7.
    • (2007) IEEE Sensors J. , vol.7 , Issue.3 , pp. 470-477
    • Wan, J.1    Shu, H.2    Huang, S.3    Fiebor, B.4    Chen, I.H.5    Petrenko, V.A.6    Chin, B.A.7
  • 271
    • 0029927067 scopus 로고    scopus 로고
    • Phage display of proteases and macromolecular inhibitors
    • Wang, C. I., Yang, Q., & Craik, C. S. (1996). Phage display of proteases and macromolecular inhibitors. Combinatorial Chemistry, 267, 52-68.
    • (1996) Combinatorial Chemistry , vol.267 , pp. 52-68
    • Wang, C.I.1    Yang, Q.2    Craik, C.S.3
  • 272
    • 0346494733 scopus 로고    scopus 로고
    • Epitope identification and discovery using phage display libraries: applications in vaccine development and diagnostics
    • Wang, L. F., & Yu, M. (2004). Epitope identification and discovery using phage display libraries: applications in vaccine development and diagnostics. Curr. Drug Targets, 5, 1-15.
    • (2004) Curr. Drug Targets , vol.5 , pp. 1-15
    • Wang, L.F.1    Yu, M.2
  • 273
    • 0028801675 scopus 로고
    • Use of a gene-targeted phage display random epitope library to map an antigenic determinant on the Bluetongue Virus outer capsid protein Vp5
    • Wang, L. F., Duplessis, D. H., White, J. R., Hyatt, A.D., & Eaton, B. T. (1995). Use of a gene-targeted phage display random epitope library to map an antigenic determinant on the Bluetongue Virus outer capsid protein Vp5. J. Immunol. Methods, 178, 1-12.
    • (1995) J. Immunol. Methods , vol.178 , pp. 1-12
    • Wang, L.F.1    Duplessis, D.H.2    White, J.R.3    Hyatt, A.D.4    Eaton, B.T.5
  • 275
    • 33744487875 scopus 로고    scopus 로고
    • Molecular imaging in cancer
    • Weissleder, R. (2006). Molecular imaging in cancer. Science, 312(5777), 1168-71.
    • (2006) Science , vol.312 , Issue.5777 , pp. 1168-1171
    • Weissleder, R.1
  • 276
    • 0034621827 scopus 로고    scopus 로고
    • Selection of peptides with semiconductor binding specificity for directed nano-crystal assembly
    • Whaley, S. R., English, D. S., Hu, E. L., Barbara, P. F., & Belcher, A. M. (2000). Selection of peptides with semiconductor binding specificity for directed nano-crystal assembly. Nature, 405, 665-8.
    • (2000) Nature , vol.405 , pp. 665-668
    • Whaley, S.R.1    English, D.S.2    Hu, E.L.3    Barbara, P.F.4    Belcher, A.M.5
  • 277
    • 0036921994 scopus 로고    scopus 로고
    • Phage display: practicalities and prospects
    • Willats, W. G. (2002). Phage display: practicalities and prospects. Plant Mol. Biol., 50, 837-54.
    • (2002) Plant Mol. Biol. , vol.50 , pp. 837-854
    • Willats, W.G.1
  • 278
    • 0031876195 scopus 로고    scopus 로고
    • Phage display: application, innovations, and issues in phage and host biology
    • Wilson, D. R., & Finlay, B. B. (1998). Phage display: application, innovations, and issues in phage and host biology. Can. J. Microbiol., 44, 313-29.
    • (1998) Can. J. Microbiol. , vol.44 , pp. 313-329
    • Wilson, D.R.1    Finlay, B.B.2
  • 279
    • 0035957374 scopus 로고    scopus 로고
    • The use of mRNA display to select high-affinity protein-binding peptides
    • Wilson, D. S., Keefe, A. D., & Szostak, J. W. (2001). The use of mRNA display to select high-affinity protein-binding peptides. Proc. Natl. Acad. Sci. USA, 98, 3750-5.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 3750-3755
    • Wilson, D.S.1    Keefe, A.D.2    Szostak, J.W.3
  • 280
    • 0033524954 scopus 로고    scopus 로고
    • Analysis of zinc fingers optimized via phage display: evaluating the utility of a recognition code
    • Wolfe, S. A., Greisman, H. A., Ramm, E. I., & Pabo, C.O. (1999). Analysis of zinc fingers optimized via phage display: evaluating the utility of a recognition code. J. Mol. Biol., 285, 1917-34.
    • (1999) J. Mol. Biol. , vol.285 , pp. 1917-1934
    • Wolfe, S.A.1    Greisman, H.A.2    Ramm, E.I.3    Pabo, C.O.4
  • 281
    • 0035793208 scopus 로고    scopus 로고
    • Stability engineering of antibody single-chain Fv fragments
    • Worn, A., & Plückthun, A. (2001). Stability engineering of antibody single-chain Fv fragments. J. Mol. Biol., 305, 989-1010.
    • (2001) J. Mol. Biol. , vol.305 , pp. 989-1010
    • Worn, A.1    Plückthun, A.2
  • 288
    • 0029896174 scopus 로고    scopus 로고
    • Affinity maturation of phage-displayed peptide ligands
    • Yu, J., & Smith, G. P. (1996). Affinity maturation of phage-displayed peptide ligands. Methods Enzymol., 267, 3-27.
    • (1996) Methods Enzymol. , vol.267 , pp. 3-27
    • Yu, J.1    Smith, G.P.2
  • 290
    • 24944535233 scopus 로고    scopus 로고
    • Molecular profiling of heart endothelial cells
    • Zhang, L., Hoffman, J. A., & Ruoslahti, E. (2005). Molecular profiling of heart endothelial cells. Circulation, 112(11), 1601-11.
    • (2005) Circulation , vol.112 , Issue.11 , pp. 1601-1611
    • Zhang, L.1    Hoffman, J.A.2    Ruoslahti, E.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.