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Volumn 69, Issue 2, 2014, Pages 109-120

Bacteriophage vehicles for phage display: Biology, mechanism, and application

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIUM ANTIBODY; COAT PROTEIN; EPITOPE; HYBRID PROTEIN; VACCINE;

EID: 84904004062     PISSN: 03438651     EISSN: 14320991     Source Type: Journal    
DOI: 10.1007/s00284-014-0557-0     Document Type: Review
Times cited : (56)

References (110)
  • 1
    • 84881575814 scopus 로고    scopus 로고
    • Production and characterization of recombinant scFv against digoxin by phage display technology
    • Alirezapour Behruz, Rajabibazl Masoumeh, Rasaee Mohhamad Javad, Omidfar K (2013) Production and characterization of recombinant scFv against digoxin by phage display technology. Monoclon Antibodies Immunodiagn Immunother 32(3):172-179
    • (2013) Monoclon Antibodies Immunodiagn Immunother , vol.32 , Issue.3 , pp. 172-179
    • Behruz, A.1    Masoumeh, R.2    Javad, R.M.3    Omidfar, K.4
  • 2
    • 0035395224 scopus 로고    scopus 로고
    • Phage display for target-based antibacterial drug discovery
    • DOI 10.1016/S1359-6446(01)01853-0, PII S1359644601018530
    • Christensen DJ, Gottlin EB, Benson RE, Hamilton PT (2001) Phage display for target-based antibacterial drug discovery. Drug Discov Today 6(14):721-727 (Pubitemid 32633919)
    • (2001) Drug Discovery Today , vol.6 , Issue.14 , pp. 721-727
    • Christensen, D.J.1    Gottlin, E.B.2    Benson, R.E.3    Hamilton, P.T.4
  • 3
    • 3342939821 scopus 로고    scopus 로고
    • Novel phage display-based subtractive screening to identify vaccine candidates of Brugia malayi
    • DOI 10.1128/IAI.72.8.4707-4715.2004
    • Gnanasekar M, Rao KVN, He YX, Mishra PK, Nutman TB, Kaliraj P, Ramaswamy K (2004) Novel phage display-based subtractive screening to identify vaccine candidates of Brugia malayi. Infect Immun 72(8):4707-4715 (Pubitemid 38989331)
    • (2004) Infection and Immunity , vol.72 , Issue.8 , pp. 4707-4715
    • Gnanasekar, M.1    Rao, K.V.N.2    He, Y.-X.3    Mishra, P.K.4    Nutman, T.B.5    Kaliraj, P.6    Ramaswamy, K.7
  • 4
    • 0346494733 scopus 로고    scopus 로고
    • Epitope identification and discovery using phage display libraries: Applications in vaccine development and diagnostics
    • Wang LF, Yu M (2004) Epitope identification and discovery using phage display libraries: applications in vaccine development and diagnostics. Curr Drug Targets 5(1):1-15
    • (2004) Curr Drug Targets , vol.5 , Issue.1 , pp. 1-15
    • Wang, L.F.1    Yu, M.2
  • 5
    • 33847138258 scopus 로고    scopus 로고
    • Production of chimeric recombinant single domain antibody-green fluorescent fusion protein in Chinese hamster ovary cells
    • DOI 10.1089/hyb.2006.037
    • Bazl MR, Rasaee M, Foruzandeh M, Rahimpour A, Kiani J, Rahbarizadeh F, Alirezapour B, Mohammadi M (2007) Production of chimeric recombinant single domain antibody-green fluorescent fusion protein in Chinese hamster ovary cells. Hybridoma 26(1):1-9 (Pubitemid 46294367)
    • (2007) Hybridoma , vol.26 , Issue.1 , pp. 1-9
    • Bazl, M.R.1    Rasaee, M.J.2    Foruzandeh, M.3    Rahimpour, A.4    Kiani, J.5    Rahbarizadeh, F.6    Alirezapour, B.7    Mohammadi, M.8
  • 9
    • 84877784402 scopus 로고    scopus 로고
    • Isolation and characterization of protective anti-LPS nanobody against V. Cholerae O1 recognizing Inaba and Ogawa serotypes
    • doi:10.1007/s00253-012-4518-x
    • Ebrahimizadeh W, Mousavi Gargari S, Rajabibazl M, Safaee Ardekani L, Zare H, Bakherad H (2013) Isolation and characterization of protective anti-LPS nanobody against V. cholerae O1 recognizing Inaba and Ogawa serotypes. Appl Microbiol Biotechnol 97(10):4457-4466. doi:10.1007/s00253-012-4518-x
    • (2013) Appl Microbiol Biotechnol , vol.97 , Issue.10 , pp. 4457-4466
    • Ebrahimizadeh, W.1    Mousavi Gargari, S.2    Rajabibazl, M.3    Safaee Ardekani, L.4    Zare, H.5    Bakherad, H.6
  • 10
    • 76649127063 scopus 로고    scopus 로고
    • New perspective for phage display as an efficient and versatile technology of functional proteomics
    • Li W, Caberoy NB (2010) New perspective for phage display as an efficient and versatile technology of functional proteomics. Appl Microbiol Biotechnol 85(4):909-919
    • (2010) Appl Microbiol Biotechnol , vol.85 , Issue.4 , pp. 909-919
    • Li, W.1    Caberoy, N.B.2
  • 12
    • 48649094750 scopus 로고    scopus 로고
    • Fully human antibodies from transgenic mouse and phage display platforms
    • Lonberg N (2008) Fully human antibodies from transgenic mouse and phage display platforms. Curr Opin Immunol 20(4):450-459
    • (2008) Curr Opin Immunol , vol.20 , Issue.4 , pp. 450-459
    • Lonberg, N.1
  • 13
    • 76249105646 scopus 로고    scopus 로고
    • Production and radioimmunoimaging of novel fully human phage display recombinant antibodies and growth inhibition of lung adenocarcinoma cell line overexpressing Prx I
    • Luo Y, Pang H, Li S, Cao H, Peng Z, Fan C (2009) Production and radioimmunoimaging of novel fully human phage display recombinant antibodies and growth inhibition of lung adenocarcinoma cell line overexpressing Prx I. Cancer Biol Ther 8(14):1369-1377
    • (2009) Cancer Biol Ther , vol.8 , Issue.14 , pp. 1369-1377
    • Luo, Y.1    Pang, H.2    Li, S.3    Cao, H.4    Peng, Z.5    Fan, C.6
  • 15
    • 0036899599 scopus 로고    scopus 로고
    • Antibody discovery: Phage display
    • DOI 10.1016/S0958-1669(02)00380-4
    • Kretzschmar T, von Rüden T (2002) Antibody discovery: phage display. Curr Opin Biotechnol 13(6):598-602 (Pubitemid 35448062)
    • (2002) Current Opinion in Biotechnology , vol.13 , Issue.6 , pp. 598-602
    • Kretzschmar, T.1    Von Ruden, T.2
  • 16
    • 68949164705 scopus 로고    scopus 로고
    • Phage display selection, analysis, and prediction of B cell epitopes
    • doi:10.1002/0471142735. im0908s86
    • Freund NT, Enshell-Seijffers D, Gershoni JM (2009) Phage display selection, analysis, and prediction of B cell epitopes. Curr Protoc Immunol 86:9.8.1-9.8.30. doi:10.1002/0471142735. im0908s86
    • (2009) Curr Protoc Immunol , vol.86
    • Freund, N.T.1    Enshell-Seijffers, D.2    Gershoni, J.M.3
  • 17
    • 79958146860 scopus 로고    scopus 로고
    • Citrulline-modified phage display: A novel high-throughput discovery approach for the identification of citrulline-containing ligands
    • doi:10.1002/pmic.201000783
    • Somers K, Stinissen P, Somers V (2011) Citrulline-modified phage display: a novel high-throughput discovery approach for the identification of citrulline-containing ligands. Proteomics 11(12):2550-2554. doi:10.1002/pmic. 201000783
    • (2011) Proteomics , vol.11 , Issue.12 , pp. 2550-2554
    • Somers, K.1    Stinissen, P.2    Somers, V.3
  • 18
    • 0036921994 scopus 로고    scopus 로고
    • Phage display: Practicalities and prospects
    • Willats WGT (2002) Phage display: practicalities and prospects. Plant Mol Biol 50(6):837-854
    • (2002) Plant Mol Biol , vol.50 , Issue.6 , pp. 837-854
    • Willats, W.G.T.1
  • 19
  • 20
    • 84863753800 scopus 로고    scopus 로고
    • A phage display-based approach to investigate abnormal neovessels of the retina
    • Staniszewska M, Gu X, Romano C, Kazlauskas A (2012) A phage display-based approach to investigate abnormal neovessels of the retina. Invest Ophthalmol Vis Sci 53(8):4371-4379
    • (2012) Invest Ophthalmol Vis Sci , vol.53 , Issue.8 , pp. 4371-4379
    • Staniszewska, M.1    Gu, X.2    Romano, C.3    Kazlauskas, A.4
  • 21
    • 79959397966 scopus 로고    scopus 로고
    • Advantages of mRNA display selections over other selection techniques for investigation of protein- protein interactions
    • Wang H, Liu R (2011) Advantages of mRNA display selections over other selection techniques for investigation of protein- protein interactions. Expert Rev Proteomics 8(3):335-346
    • (2011) Expert Rev Proteomics , vol.8 , Issue.3 , pp. 335-346
    • Wang, H.1    Liu, R.2
  • 22
    • 84865640453 scopus 로고    scopus 로고
    • Advances in the production of human monoclonal antibodies
    • Wang S (2011) Advances in the production of human monoclonal antibodies. Antib Technol J 1:1-4
    • (2011) Antib Technol J , vol.1 , pp. 1-4
    • Wang, S.1
  • 23
    • 77949886815 scopus 로고    scopus 로고
    • Progress in phage display: Evolution of the technique and its applications
    • Bratkovič T (2010) Progress in phage display: evolution of the technique and its applications. Cell Mol Life Sci 67(5):749-767
    • (2010) Cell Mol Life Sci , vol.67 , Issue.5 , pp. 749-767
    • Bratkovič, T.1
  • 24
    • 43449114509 scopus 로고    scopus 로고
    • Monoclonal antibodies in clinical diagnosis: A brief review application
    • Saleem M, Mustafa K (2010) Monoclonal antibodies in clinical diagnosis: a brief review application. Afr J Biotechnol 7(8):923-925 (Pubitemid 351669255)
    • (2008) African Journal of Biotechnology , vol.7 , Issue.8 , pp. 923-925
    • Saleem, M.1    Kamal, M.2
  • 25
    • 76549113580 scopus 로고    scopus 로고
    • Construction and quality examination of murine naive T7 phage display antibody library
    • Du XJ, Wu YN, Zhang WW, Dong F, Wang S (2010) Construction and quality examination of murine naive T7 phage display antibody library. Food Agric Immunol 21(1):81-90
    • (2010) Food Agric Immunol , vol.21 , Issue.1 , pp. 81-90
    • Du, X.J.1    Wu, Y.N.2    Zhang, W.W.3    Dong, F.4    Wang, S.5
  • 26
    • 77955663582 scopus 로고    scopus 로고
    • Selection of single chain variable fragment (scFv) antibodies from a hyperimmunized phage display library for the detection of the antibiotic monensin
    • Makvandi-Nejad S, Sheedy C, Veldhuis L, Richard G, Hall JC (2010) Selection of single chain variable fragment (scFv) antibodies from a hyperimmunized phage display library for the detection of the antibiotic monensin. J ImmunolMethods 360(1-2):103-118
    • (2010) J ImmunolMethods , vol.360 , Issue.1-2 , pp. 103-118
    • Makvandi-Nejad, S.1    Sheedy, C.2    Veldhuis, L.3    Richard, G.4    Hall, J.C.5
  • 27
    • 84871649282 scopus 로고    scopus 로고
    • Construction of an artificially randomized IgNAR phage display library: Screening of variable regions that bind to hen egg white lysozyme
    • doi:10.1007/s10126-012-9456-1
    • Ohtani M, Hikima J, Jung TS, Kondo H, Hirono I, Aoki T (2013) Construction of an artificially randomized IgNAR phage display library: screening of variable regions that bind to hen egg white lysozyme. Mar Biotechnol 15(1):56-62. doi:10.1007/s10126-012-9456-1
    • (2013) Mar Biotechnol , vol.15 , Issue.1 , pp. 56-62
    • Ohtani, M.1    Hikima, J.2    Jung, T.S.3    Kondo, H.4    Hirono, I.5    Aoki, T.6
  • 28
    • 79955650818 scopus 로고    scopus 로고
    • A novel synthetic naïve human antibody library allows the isolation of antibodies against a new epitope of oncofetal fibronectin
    • Villa A, Lovato V, Bujak E, Wulhfard S, Pasche N, Neri D (2011) A novel synthetic naïve human antibody library allows the isolation of antibodies against a new epitope of oncofetal fibronectin. MAbs 3:264-272
    • (2011) MAbs , vol.3 , pp. 264-272
    • Villa, A.1    Lovato, V.2    Bujak, E.3    Wulhfard, S.4    Pasche, N.5    Neri, D.6
  • 29
    • 34547515975 scopus 로고    scopus 로고
    • The rapid discovery of engineered antibodies
    • Wang M, He M (2007) The rapid discovery of engineered antibodies. IDrugs 10(8):562
    • (2007) IDrugs , vol.10 , Issue.8 , pp. 562
    • Wang, M.1    He, M.2
  • 30
    • 0031081318 scopus 로고    scopus 로고
    • Designing and optimizing library selection strategies for generating high-affinity antibodies
    • Hoogenboom HR (1997) Designing and optimizing library selection strategies for generating high-affinity antibodies. Trends Biotechnol 15(2):62-70
    • (1997) Trends Biotechnol , vol.15 , Issue.2 , pp. 62-70
    • Hoogenboom, H.R.1
  • 31
    • 0035885270 scopus 로고    scopus 로고
    • Evidence for a bias toward intracellular antigens in the local humoral anti-tumor immune response of a colorectal cancer patient revealed by phage display
    • DOI 10.1002/ijc.1382
    • Roovers RC, van der Linden E, Zijlema H, de Bruïne A, Arends JW, Hoogenboom HR (2001) Evidence for a bias toward intracellular antigens in the local humoral anti-tumor immune response of a colorectal cancer patient revealed by phage display. Int J Cancer 93(6):832-840 (Pubitemid 32756753)
    • (2001) International Journal of Cancer , vol.93 , Issue.6 , pp. 832-840
    • Roovers, R.C.1    Van Der, L.E.2    Zijlema, H.3    De Brune, A.4    Arends, J.-W.5    Hoogenboom, H.R.6
  • 32
    • 79959221560 scopus 로고    scopus 로고
    • Reversible and irreversible protein glutathionylation: Biological and clinical aspects
    • doi:10.1517/17425255.2011.577738
    • Cooper AJL, Pinto JT, Callery PS (2011) Reversible and irreversible protein glutathionylation: biological and clinical aspects. Expert Opin Drug Metab Toxicol 7(7):891-910. doi:10.1517/17425255.2011.577738
    • (2011) Expert Opin Drug Metab Toxicol , vol.7 , Issue.7 , pp. 891-910
    • Cooper, A.J.L.1    Pinto, J.T.2    Callery, P.S.3
  • 33
    • 79955529483 scopus 로고    scopus 로고
    • Lambda-display: A powerful tool for antigen discovery
    • Beghetto E, Gargano N (2011) Lambda-display: a powerful tool for antigen discovery. Molecules 16(4):3089-3105
    • (2011) Molecules , vol.16 , Issue.4 , pp. 3089-3105
    • Beghetto, E.1    Gargano, N.2
  • 36
    • 63749122530 scopus 로고    scopus 로고
    • Molecular modification of T4 bacteriophage proteins and its potential application - Review
    • Kurzȩpa A, Da̧browska K, Świtała-Jeleń K, Górski A (2009) Molecular modification of T4 bacteriophage proteins and its potential application - review. Folia Microbiol 54(1):5-15
    • (2009) Folia Microbiol , vol.54 , Issue.1 , pp. 5-15
    • Kurzȩpa, A.1    Da̧browska, K.2    Świtała-Jeleń, K.3    Górski, A.4
  • 38
    • 21644456591 scopus 로고    scopus 로고
    • Phage display vectors for the in vitro generation of human antibody fragments
    • Burns R (ed) Humana Press
    • Hust M, Dübel S (2005) Phage display vectors for the in vitro generation of human antibody fragments. In: Burns R (ed) Immunochemical protocols. Methods in molecular biology, vol 295. Humana Press, pp 71-96
    • (2005) Immunochemical Protocols. Methods in Molecular Biology , vol.295 , pp. 71-96
    • Hust, M.1    Dübel, S.2
  • 39
    • 32544440280 scopus 로고    scopus 로고
    • Phage display systems and their applications
    • Paschke M (2006) Phage display systems and their applications. Appl Microbiol Biotechnol 70(1):2-11
    • (2006) Appl Microbiol Biotechnol , vol.70 , Issue.1 , pp. 2-11
    • Paschke, M.1
  • 41
    • 84897469674 scopus 로고    scopus 로고
    • Phage display on the base of filamentous bacteriophages: Application for recombinant antibodies selection
    • Tikunova N, Morozova V (2009) Phage display on the base of filamentous bacteriophages: application for recombinant antibodies selection. Acta Naturae 1(3):20
    • (2009) Acta Naturae , vol.1 , Issue.3 , pp. 20
    • Tikunova, N.1    Morozova, V.2
  • 42
    • 0031876195 scopus 로고    scopus 로고
    • Phage display: Applications, innovations, and issues in phage and host biology
    • Wilson DR, Finlay BB (1998) Phage display: applications, innovations, and issues in phage and host biology. Can J Microbiol 44(4):313-329
    • (1998) Can J Microbiol , vol.44 , Issue.4 , pp. 313-329
    • Wilson, D.R.1    Finlay, B.B.2
  • 44
    • 10144231462 scopus 로고    scopus 로고
    • Phage display: A molecular tool for the generation of antibodies - A review
    • Schmitz U, Versmold A, Kaufmann P, Frank HG (2000) Phage display: a molecular tool for the generation of antibodies - a review. Placenta 21:S106-S112
    • (2000) Placenta , vol.21
    • Schmitz, U.1    Versmold, A.2    Kaufmann, P.3    Frank, H.G.4
  • 45
    • 33645463597 scopus 로고    scopus 로고
    • Bacteriophage replication modules
    • Weigel C, Seitz H (2006) Bacteriophage replication modules. FEMS Microbiol Rev 30(3):321-381
    • (2006) FEMS Microbiol Rev , vol.30 , Issue.3 , pp. 321-381
    • Weigel, C.1    Seitz, H.2
  • 48
    • 0032901290 scopus 로고    scopus 로고
    • Phage-display technology - Finding a needle in a vast molecular haystack
    • DOI 10.1016/S0958-1669(99)80016-0
    • Rodi DJ, Makowski L (1999) Phage-display technology - finding a needle in a vast molecular haystack. Curr Opin Biotechnol 10(1):87-93 (Pubitemid 29054632)
    • (1999) Current Opinion in Biotechnology , vol.10 , Issue.1 , pp. 87-93
    • Rodi, D.J.1    Makowski, L.2
  • 49
    • 0034887457 scopus 로고    scopus 로고
    • Engineering M13 for phage display
    • Sidhu SS (2001) Engineering M13 for phage display. Biomol Eng 18(2):57-63
    • (2001) Biomol Eng , vol.18 , Issue.2 , pp. 57-63
    • Sidhu, S.S.1
  • 51
    • 0035818507 scopus 로고    scopus 로고
    • T7 phage display: A novel genetic selection system for cloning RNA-binding proteins from cDNA libraries
    • Danner S, Belasco JG (2001) T7 phage display: a novel genetic selection system for cloning RNA-binding proteins from cDNA libraries. Proc Natl Acad Sci 98(23):12954
    • (2001) Proc Natl Acad Sci , vol.98 , Issue.23 , pp. 12954
    • Danner, S.1    Belasco, J.G.2
  • 52
    • 0034141510 scopus 로고    scopus 로고
    • The efficiency of Escherichia coli selenocysteine insertion is influenced by the immediate downstream nucleotide
    • Sandman KE, Noren CJ (2000) The efficiency of Escherichia coli selenocysteine insertion is influenced by the immediate downstream nucleotide. Nucleic Acids Res 28(3):755-761 (Pubitemid 30068259)
    • (2000) Nucleic Acids Research , vol.28 , Issue.3 , pp. 755-761
    • Sandman, K.E.1    Noren, C.J.2
  • 53
    • 44049095603 scopus 로고    scopus 로고
    • SRP and Sec pathway leader peptides for antibody phage display and antibody fragment production in E. coli
    • DOI 10.1016/j.nbt.2008.01.001, PII S1871678408000022
    • Thie H, Schirrmann T, Paschke M, Dübel S, Hust M (2008) SRP and Sec pathway leader peptides for antibody phage display and antibody fragment production in E. coli. New Biotechnol 25(1):49-54 (Pubitemid 351713600)
    • (2008) New Biotechnology , vol.25 , Issue.1 , pp. 49-54
    • Thie, H.1    Schirrmann, T.2    Paschke, M.3    Dubel, S.4    Hust, M.5
  • 54
    • 0035853288 scopus 로고    scopus 로고
    • Selection of ligands by panning of domain libraries displayed on phage lambda reveals new potential partners of synaptojanin 1
    • DOI 10.1006/jmbi.2001.4572
    • Zucconi A, Dente L, Santonico E, Castagnoli L, Cesareni G (2001) Selection of ligands by panning of domain libraries displayed on phage lambda reveals new potential partners of synaptojanin 1. J Mol Biol 307(5):1329-1339 (Pubitemid 33027643)
    • (2001) Journal of Molecular Biology , vol.307 , Issue.5 , pp. 1329-1339
    • Zucconi, A.1    Dente, L.2    Santonico, E.3    Castagnoli, L.4    Cesareni, G.5
  • 55
    • 0035500462 scopus 로고    scopus 로고
    • T7 displayed peptides as targets for selecting peptide specific scFvs from M13 scFv display libraries
    • DOI 10.1016/S0022-1759(01)00454-9, PII S0022175901004549
    • Castillo J, Goodson B, Winter J (2001) T7 displayed peptides as targets for selecting peptide specific scFvs from M13 scFv display libraries. J Immunol Methods 257(1-2):117-122 (Pubitemid 33001239)
    • (2001) Journal of Immunological Methods , vol.257 , Issue.1-2 , pp. 117-122
    • Castillo, J.1    Goodson, B.2    Winter, J.3
  • 56
    • 79953106017 scopus 로고    scopus 로고
    • Bacteriophage assembly
    • Aksyuk AA, Rossmann MG (2011) Bacteriophage assembly. Viruses 3(3):172-203
    • (2011) Viruses , vol.3 , Issue.3 , pp. 172-203
    • Aksyuk, A.A.1    Rossmann, M.G.2
  • 57
    • 12244258510 scopus 로고    scopus 로고
    • Experimental evolution of conflict mediation between genomes
    • Sachs JL, Bull JJ (2005) Experimental evolution of conflict mediation between genomes. Proc Natl Acad Sci USA 102(2):390
    • (2005) Proc Natl Acad Sci USA , vol.102 , Issue.2 , pp. 390
    • Sachs, J.L.1    Bull, J.J.2
  • 58
    • 84857642791 scopus 로고    scopus 로고
    • Phagemid vectors for phage display: Properties, characteristics and construction
    • Qi H, Lu H, Qiu HJ, Petrenko V, Liu A (2012) Phagemid vectors for phage display: properties, characteristics and construction. J Mol Biol 417:129-143
    • (2012) J Mol Biol , vol.417 , pp. 129-143
    • Qi, H.1    Lu, H.2    Qiu, H.J.3    Petrenko, V.4    Liu, A.5
  • 59
    • 0036511677 scopus 로고    scopus 로고
    • An improved helper phage system for efficient isolation of specific antibody molecules in phage display
    • Baek H, Suk K, Kim Y, Cha S (2002) An improved helper phage system for efficient isolation of specific antibody molecules in phage display. Nucleic Acids Res 30(5):e18
    • (2002) Nucleic Acids Res , vol.30 , Issue.5
    • Baek, H.1    Suk, K.2    Kim, Y.3    Cha, S.4
  • 61
    • 0035169340 scopus 로고    scopus 로고
    • A helper phage to improve single-chain antibody presentation in phage display
    • DOI 10.1038/83567
    • Rondot S, Koch J, Breitling F, Dübel S (2001) A helper phage to improve single-chain antibody presentation in phage display. Nat Biotechnol 19(1):75-78 (Pubitemid 32051961)
    • (2001) Nature Biotechnology , vol.19 , Issue.1 , pp. 75-78
    • Rondot, S.1    Koch, J.2    Breitling, F.3    Dubel, S.4
  • 62
    • 0037374091 scopus 로고    scopus 로고
    • A new helper phage and phagemid vector system improves viral display of antibody Fab fragments and avoids propagation of insert-less virions
    • DOI 10.1016/S0022-1759(02)00294-6, PII S0022175902002946
    • Soltes G, Barker H, Marmai K, Pun E, Yuen A, Wiersma EJ (2003) A new helper phage and phagemid vector system improves viral display of antibody Fab fragments and avoids propagation of insertless virions. J Immunol Methods 274(1):233-244 (Pubitemid 36263059)
    • (2003) Journal of Immunological Methods , vol.274 , Issue.1-2 , pp. 233-244
    • Soltes, G.1    Barker, H.2    Marmai, K.3    Pun, E.4    Yuen, A.5    Wiersma, E.J.6
  • 63
    • 0004161721 scopus 로고    scopus 로고
    • The bacteriophages
    • Calendar R (ed) Oxford University Press, New York
    • Calendar R (2006) The bacteriophages. In: Calendar R (ed) The bacteriophages. Oxford University Press, New York
    • (2006) The Bacteriophages
    • Calendar, R.1
  • 66
    • 84858701467 scopus 로고    scopus 로고
    • Lambda genomic DNA quantification using ultrasonic treatment followed by liquid chromatography-isotope dilution mass spectrometry
    • doi:10.1007/s00216-011-5644-5
    • Dong L, Zang C, Wang J, Li L, Gao Y, Wu L, Li P (2012) Lambda genomic DNA quantification using ultrasonic treatment followed by liquid chromatography-isotope dilution mass spectrometry. Anal Bioanal Chem 402(6):2079-2088. doi:10.1007/s00216-011-5644-5
    • (2012) Anal Bioanal Chem , vol.402 , Issue.6 , pp. 2079-2088
    • Dong, L.1    Zang, C.2    Wang, J.3    Li, L.4    Gao, Y.5    Wu, L.6    Li, P.7
  • 67
    • 58149520031 scopus 로고    scopus 로고
    • Genomic characterization of Ralstonia solanacearum phage URSB1, a T7-like wide-host-range phage
    • Kawasaki T, Shimizu M, Satsuma H, Fujiwara A, Fujie M, Usami S, Yamada T (2009) Genomic characterization of Ralstonia solanacearum phage URSB1, a T7-like wide-host-range phage. J Bacteriol 191(1):422-427
    • (2009) J Bacteriol , vol.191 , Issue.1 , pp. 422-427
    • Kawasaki, T.1    Shimizu, M.2    Satsuma, H.3    Fujiwara, A.4    Fujie, M.5    Usami, S.6    Yamada, T.7
  • 68
    • 78649623974 scopus 로고    scopus 로고
    • Structure and assembly of bacteriophage T4 head
    • Rao VB, Black LW (2010) Structure and assembly of bacteriophage T4 head. Virol J 7(1):356
    • (2010) Virol J , vol.7 , Issue.1 , pp. 356
    • Rao, V.B.1    Black, L.W.2
  • 69
    • 73649087232 scopus 로고    scopus 로고
    • Structure of the small outer capsid protein, Soc: A clamp for stabilizing capsids of T4-like phages
    • Qin L, Fokine A, O'Donnell E, Rao VB, Rossmann MG (2010) Structure of the small outer capsid protein, Soc: a clamp for stabilizing capsids of T4-like phages. J Mol Biol 395(4):728-741
    • (2010) J Mol Biol , vol.395 , Issue.4 , pp. 728-741
    • Qin, L.1    Fokine, A.2    O'Donnell, E.3    Rao, V.B.4    Rossmann, M.G.5
  • 70
    • 0035864288 scopus 로고    scopus 로고
    • The structure of isometric capsids of bacteriophage T4
    • DOI 10.1006/viro.2000.0735
    • Olson NH, Gingery M, Eiserling FA, Baker TS (2001) The structure of isometric capsids of bacteriophage T4. Virology 279(2):385-391 (Pubitemid 34161102)
    • (2001) Virology , vol.279 , Issue.2 , pp. 385-391
    • Olson, N.H.1    Gingery, M.2    Eiserling, F.A.3    Baker, T.S.4
  • 74
    • 77954368167 scopus 로고    scopus 로고
    • Functional analysis of the highly antigenic outer capsid protein, Hoc, a virus decoration protein from T4-like bacteriophages
    • Sathaliyawala T, Islam MZ, Li Q, Fokine A, Rossmann MG, Rao VB (2010) Functional analysis of the highly antigenic outer capsid protein, Hoc, a virus decoration protein from T4-like bacteriophages. Mol Microbiol 77(2):444-455
    • (2010) Mol Microbiol , vol.77 , Issue.2 , pp. 444-455
    • Sathaliyawala, T.1    Islam, M.Z.2    Li, Q.3    Fokine, A.4    Rossmann, M.G.5    Rao, V.B.6
  • 75
    • 84904007976 scopus 로고    scopus 로고
    • Method for making an immunogenic composition with Hoc fusion proteins and/or Soc fusion proteins
    • EP Patent 2(196):214
    • Rao VB (2010) Method for making an immunogenic composition with Hoc fusion proteins and/or Soc fusion proteins. EP Patent 2(196):214
    • (2010)
    • Rao, V.B.1
  • 76
    • 84903935765 scopus 로고    scopus 로고
    • Phage display of intact domains at high copy number
    • USA Patent US 20060068379 A1
    • Steven AC, Wingfield PT, Black LW, Ren Z (2006) Phage display of intact domains at high copy number. USA Patent US 20060068379 A1
    • (2006)
    • Steven, A.C.1    Wingfield, P.T.2    Black, L.W.3    Ren, Z.4
  • 78
    • 33748920016 scopus 로고    scopus 로고
    • Bacteriophage T4 Capsid: A Unique Platform for Efficient Surface Assembly of Macromolecular Complexes
    • DOI 10.1016/j.jmb.2006.08.049, PII S0022283606010758
    • Li Q, Shivachandra SB, Leppla SH, Rao VB (2006) Bacteriophage T4 capsid: a unique platform for efficient surface assembly of macromolecular complexes. J Mol Biol 363(2):577-588 (Pubitemid 44436261)
    • (2006) Journal of Molecular Biology , vol.363 , Issue.2 , pp. 577-588
    • Li, Q.1    Shivachandra, S.B.2    Leppla, S.H.3    Rao, V.B.4
  • 79
    • 30844452698 scopus 로고    scopus 로고
    • In vitro binding of anthrax protective antigen on bacteriophage T4 capsid surface through Hoc-capsid interactions: A strategy for efficient display of large full-length proteins
    • DOI 10.1016/j.virol.2005.10.037, PII S0042682205006719
    • Shivachandra SB, Rao M, Janosi L, Sathaliyawala T, Matyas GR, Alving CR, Leppla SH, Rao VB (2006) In vitro binding of anthrax protective antigen on bacteriophage T4 capsid surface through Hoc-capsid interactions: a strategy for efficient display of large full-length proteins. Virology 345(1):190-198 (Pubitemid 43107584)
    • (2006) Virology , vol.345 , Issue.1 , pp. 190-198
    • Shivachandra, S.B.1    Rao, M.2    Janosi, L.3    Sathaliyawala, T.4    Matyas, G.R.5    Alving, C.R.6    Leppla, S.H.7    Rao, V.B.8
  • 80
    • 0042827209 scopus 로고    scopus 로고
    • Molecular mechanisms in bacteriophage T7 procapsid assembly, maturation, and DNA containment
    • DOI 10.1016/S0065-3233(03)01008-8
    • Cerritelli ME, Conway JF, Cheng N, Trus BL, Steven AC (2003) Molecular mechanisms in bacteriophage T7 procapsid assembly, maturation, and DNA containment. Adv Protein Chem 64:301-323 (Pubitemid 37070659)
    • (2003) Advances in Protein Chemistry , vol.64 , pp. 301-323
    • Cerritelli, M.E.1    Conway, J.F.2    Cheng, N.3    Trus, B.L.4    Steven, A.C.5
  • 81
    • 75849141082 scopus 로고    scopus 로고
    • Gp15 and gp16 cooperate in translocating bacteriophage T7 DNA into the infected cell
    • Chang CY, Kemp P, Molineux IJ (2010) Gp15 and gp16 cooperate in translocating bacteriophage T7 DNA into the infected cell. Virology 398(2):176-186
    • (2010) Virology , vol.398 , Issue.2 , pp. 176-186
    • Chang, C.Y.1    Kemp, P.2    Molineux, I.J.3
  • 82
    • 80051788970 scopus 로고    scopus 로고
    • Bacteriophage-host interactions leading to genome internalization
    • doi:10.1016/j.mib.2011.07.010
    • Bertin A, de Frutos M, Letellier L (2011) Bacteriophage-host interactions leading to genome internalization. Curr Opin Microbiol 14(4):492-496. doi:10.1016/j.mib.2011.07.010
    • (2011) Curr Opin Microbiol , vol.14 , Issue.4 , pp. 492-496
    • Bertin, A.1    De Frutos, M.2    Letellier, L.3
  • 84
    • 84862233134 scopus 로고    scopus 로고
    • Structure of the receptorbinding carboxy-terminal domain of bacteriophage T7 tail fibers
    • Garcia-Doval C, van Raaij MJ (2012) Structure of the receptorbinding carboxy-terminal domain of bacteriophage T7 tail fibers. Proc Natl Acad Sci 109(24):9390-9395
    • (2012) Proc Natl Acad Sci , vol.109 , Issue.24 , pp. 9390-9395
    • Garcia-Doval, C.1    Van Raaij, M.J.2
  • 85
    • 34347354221 scopus 로고    scopus 로고
    • Testing optimality with experimental evolution: Lysis time in a bacteriophage
    • DOI 10.1111/j.1558-5646.2007.00132.x
    • Heineman RH, Bull JJ (2007) Testing optimality with experimental evolution: lysis time in a bacteriophage. Evolution 61(7):1695-1709 (Pubitemid 47013467)
    • (2007) Evolution , vol.61 , Issue.7 , pp. 1695-1709
    • Heineman, R.H.1    Bull, J.J.2
  • 88
    • 61849155151 scopus 로고    scopus 로고
    • The phage k major tail protein structure reveals a common evolution for long-tailed phages and the type VI bacterial secretion system
    • Pell LG, Kanelis V, Donaldson LW, Lynne Howell P, Davidson AR (2009) The phage k major tail protein structure reveals a common evolution for long-tailed phages and the type VI bacterial secretion system. Proc Natl Acad Sci 106(11):4160
    • (2009) Proc Natl Acad Sci , vol.106 , Issue.11 , pp. 4160
    • Pell, L.G.1    Kanelis, V.2    Donaldson, L.W.3    Lynne Howell, P.4    Davidson, A.R.5
  • 89
    • 84863393863 scopus 로고    scopus 로고
    • Repeatability and contingency in the evolution of a key innovation in phage lambda
    • Meyer JR, Dobias DT, Weitz JS, Barrick JE, Quick RT, Lenski RE (2012) Repeatability and contingency in the evolution of a key innovation in phage lambda. Science 335(6067):428-432
    • (2012) Science , vol.335 , Issue.6067 , pp. 428-432
    • Meyer, J.R.1    Dobias, D.T.2    Weitz, J.S.3    Barrick, J.E.4    Quick, R.T.5    Lenski, R.E.6
  • 91
    • 62449181292 scopus 로고    scopus 로고
    • Determining DNA packaging strategy by analysis of the termini of the chromosomes in tailed-bacteriophage virions
    • Casjens SR, Gilcrease EB (2009) Determining DNA packaging strategy by analysis of the termini of the chromosomes in tailed-bacteriophage virions. Methods Mol Biol 502:91-111
    • (2009) Methods Mol Biol , vol.502 , pp. 91-111
    • Casjens, S.R.1    Gilcrease, E.B.2
  • 93
    • 0028168581 scopus 로고
    • Lambda foo: A lambda phage vector for the expression of foreign proteins
    • Maruyama IN, Maruyama HI, Brenner S (1994) Lambda foo: a lambda phage vector for the expression of foreign proteins. Proc Natl Acad Sci 91(17):8273
    • (1994) Proc Natl Acad Sci , vol.91 , Issue.17 , pp. 8273
    • Maruyama, I.N.1    Maruyama, H.I.2    Brenner, S.3
  • 94
    • 0036122939 scopus 로고    scopus 로고
    • Bacteriophage lambda as a vehicle for peptide and protein display
    • Hoess RH (2002) Bacteriophage lambda as a vehicle for peptide and protein display. Curr Pharm Biotechnol 3(1):23-28
    • (2002) Curr Pharm Biotechnol , vol.3 , Issue.1 , pp. 23-28
    • Hoess, R.H.1
  • 95
    • 0030582396 scopus 로고    scopus 로고
    • Surface display of proteins on bacteriophage lambda heads
    • DOI 10.1006/jmbi.1996.0495
    • Gi Mikawa Y, Maruyama IN, Brenner S (1996) Surface display of proteins on bacteriophage (lambda) heads. J Mol Biol 262(1):21-30 (Pubitemid 26315989)
    • (1996) Journal of Molecular Biology , vol.262 , Issue.1 , pp. 21-30
    • Mikawa, Y.G.1    Maruyama, I.N.2    Brenner, S.3
  • 96
    • 0035853288 scopus 로고    scopus 로고
    • Selection of ligands by panning of domain libraries displayed on phage lambda reveals new potential partners of synaptojanin 1
    • DOI 10.1006/jmbi.2001.4572
    • Zucconi A, Dente L, Santonico E, Castagnoli L, Cesareni G (2001) Selection of ligands by panning of domain libraries displayed on phage lambda reveals new potential partners of synaptojanin 11. J Mol Biol 307(5):1329-1339 (Pubitemid 33027643)
    • (2001) Journal of Molecular Biology , vol.307 , Issue.5 , pp. 1329-1339
    • Zucconi, A.1    Dente, L.2    Santonico, E.3    Castagnoli, L.4    Cesareni, G.5
  • 97
    • 84872224887 scopus 로고    scopus 로고
    • Phage display - A powerful technique for immunotherapy: 2. Vaccine delivery
    • Bazan J, Całkosiński I, Gamian A (2012) Phage display - a powerful technique for immunotherapy: 2. Vaccine delivery. Hum Vaccin Immunother 8(12):1829-1835
    • (2012) Hum Vaccin Immunother , vol.8 , Issue.12 , pp. 1829-1835
    • Bazan, J.1    Całkosiński, I.2    Gamian, A.3
  • 99
    • 0034812728 scopus 로고    scopus 로고
    • Isolation of human antibodies against the central DNA binding domain of p53 from an individual with colorectal cancer using antibody phage display
    • Coomber DW, Ward RL (2001) Isolation of human antibodies against the central DNA binding domain of p53 from an individual with colorectal cancer using antibody phage display. Clin Cancer Res 7(9):2802-2808 (Pubitemid 32911388)
    • (2001) Clinical Cancer Research , vol.7 , Issue.9 , pp. 2802-2808
    • Coomber, D.W.J.1    Ward, R.L.2
  • 100
    • 22244433830 scopus 로고    scopus 로고
    • A mimotope peptide-based anti-cancer vaccine selected by BAT monoclonal antibody
    • DOI 10.1016/j.vaccine.2005.04.009, PII S0264410X05004378
    • Hardy B, Raiter A (2005) A mimotope peptide-based anti-cancer vaccine selected by BAT monoclonal antibody. Vaccine 23(34):4283-4291 (Pubitemid 40991232)
    • (2005) Vaccine , vol.23 , Issue.34 , pp. 4283-4291
    • Hardy, B.1    Raiter, A.2
  • 102
  • 104
    • 77953284751 scopus 로고    scopus 로고
    • Mapping of Taenia solium TSOL18 antigenic epitopes by phage display library
    • Guo A, Cai X, Jia W, Liu B, Zhang S, Wang P, Yan H, Luo X (2010) Mapping of Taenia solium TSOL18 antigenic epitopes by phage display library. Parasitol Res 106(5):1151-1157
    • (2010) Parasitol Res , vol.106 , Issue.5 , pp. 1151-1157
    • Guo, A.1    Cai, X.2    Jia, W.3    Liu, B.4    Zhang, S.5    Wang, P.6    Yan, H.7    Luo, X.8
  • 105
    • 84866497183 scopus 로고    scopus 로고
    • Epitope mapping by random peptide phage display reveals essential residues for vaccinia extracellular enveloped virion spread
    • He Y, Wang Y, Struble EB, Zhang P, Chowdhury S, Reed JL, Kennedy M, Scott DE, Fisher RW (2012) Epitope mapping by random peptide phage display reveals essential residues for vaccinia extracellular enveloped virion spread. Virol J 9(1):217
    • (2012) Virol J , vol.9 , Issue.1 , pp. 217
    • He, Y.1    Wang, Y.2    Struble, E.B.3    Zhang, P.4    Chowdhury, S.5    Reed, J.L.6    Kennedy, M.7    Scott, D.E.8    Fisher, R.W.9
  • 106
    • 78650055406 scopus 로고    scopus 로고
    • High-resolution epitope mapping for monoclonal antibodies to the structural protein erns of classical swine fever virus using peptide array and random peptide phage display approaches
    • Lin M, McRae H, Dan H, Tangorra E, Laverdiere A, Pasick J (2010) High-resolution epitope mapping for monoclonal antibodies to the structural protein erns of classical swine fever virus using peptide array and random peptide phage display approaches. J Gen Virol 91(12):2928-2940
    • (2010) J Gen Virol , vol.91 , Issue.12 , pp. 2928-2940
    • Lin, M.1    McRae, H.2    Dan, H.3    Tangorra, E.4    Laverdiere, A.5    Pasick, J.6
  • 107
    • 77951190947 scopus 로고    scopus 로고
    • A comprehensive analysis of filamentous phage display vectors for cytoplasmic proteins: An analysis with different fluorescent proteins
    • doi:10.1093/nar/gkp809
    • Velappan N, Fisher HE, Pesavento E, Chasteen L, D'Angelo S, Kiss C, Longmire M, Pavlik P, Bradbury ARM (2010) A comprehensive analysis of filamentous phage display vectors for cytoplasmic proteins: an analysis with different fluorescent proteins. Nucleic Acids Res 38(4):e22. doi:10.1093/nar/gkp809
    • (2010) Nucleic Acids Res , vol.38 , Issue.4
    • Velappan, N.1    Fisher, H.E.2    Pesavento, E.3    Chasteen, L.4    D'Angelo, S.5    Kiss, C.6    Longmire, M.7    Pavlik, P.8    Bradbury, A.R.M.9
  • 108
    • 0034681299 scopus 로고    scopus 로고
    • High copy display of large proteins on phage for functional selections
    • doi:10.1006/jmbi.1999.346
    • Sidhu SS, Weiss GA, Wells JA (2000) High copy display of large proteins on phage for functional selections. J Mol Biol 296(2):487-495. doi:10.1006/jmbi.1999.346
    • (2000) J Mol Biol , vol.296 , Issue.2 , pp. 487-495
    • Sidhu, S.S.1    Weiss, G.A.2    Wells, J.A.3
  • 109
    • 21644456591 scopus 로고    scopus 로고
    • Immunochemical protocols
    • Burns R (ed), Humana Press, doi:10.1385/1-59259-873-0:071
    • Immunochemical protocols. In: Burns R (ed), vol 295. Methods in molecular biology. Humana Press, pp 71-96. doi:10.1385/1-59259-873-0:071
    • Methods in Molecular Biology , vol.295 , pp. 71-96
  • 110
    • 0012352746 scopus 로고    scopus 로고
    • Analysis of bacteriophage T4 based on the completed DNA sequence
    • Kutter E (1996) Analysis of bacteriophage T4 based on the completed DNA sequence. In: Integrative approaches to molecular biology, pp 13-28
    • (1996) Integrative Approaches to Molecular Biology , pp. 13-28
    • Kutter, E.1


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