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1
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0026437442
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Identification of novel peptide antagonists for GPIIb/IIIa from a conformationally constrained phage peptide library
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2
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0027158405
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Mimicking of discontinuous epitopes by phage-displayed peptides. I. Epitope mapping of human H ferritin using a phage library of constrained peptides
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Luzzago A, Felici F, Tramontano A, Pessi A, Cortese R. Mimicking of discontinuous epitopes by phage-displayed peptides. I. Epitope mapping of human H ferritin using a phage library of constrained peptides. Gene. 128:1993;51-57.
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Luzzago, A.1
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4
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0028304495
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Identification of a structural epitope by using a peptide library displayed on filamentous bacteriophage
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Hoess RH, Mack AJ, Walton H, Reilly TM. Identification of a structural epitope by using a peptide library displayed on filamentous bacteriophage. J Immunol. 153:1994;724-729.
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Hoess, R.H.1
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0029920670
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Probing the basis of antibody reactivity with a panel of constrained peptide libraries displayed by filamentous phage
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Bonnycastle LLC, Mehroke JS, Rashed M, Gong X, Scott JK. Probing the basis of antibody reactivity with a panel of constrained peptide libraries displayed by filamentous phage. J Mol Biol. 258:1996;747-762.
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6
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The affinity-selection of a minibody polypeptide inhibitor of human interleukin-6
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Martin F, Toniatti C, Salvati AL, Venturini S, Ciliberto G, Cortese R, Sollazzo M. The affinity-selection of a minibody polypeptide inhibitor of human interleukin-6. EMBO J. 13:1994;5303-5309.
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Martin, F.1
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7
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Tendamistat as a scaffold for conformationally constrained phage peptide libraries
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McConnell S, Hoess RH. Tendamistat as a scaffold for conformationally constrained phage peptide libraries. J Mol Biol. 250:1995;460-470.
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McConnell, S.1
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8
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0028902841
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A conformationally homogenous combinatorial peptide library
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Bianchi E, Folgori A, Wallace A, Nicotra M, Acali S, Phalipon A, Barbato G, Bazzo R, Cortese R, Felici F, Pessi A. A conformationally homogenous combinatorial peptide library. J Mol Biol. 247:1995;154-160.
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Bianchi, E.1
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9
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0028982245
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A combinatorial library of an α-helical bacterial receptor domain
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Nord K, Nilsson J, Nilsson B, Uhlén M, Nygren P-Å. A combinatorial library of an α-helical bacterial receptor domain. Protein Eng. 8:1995;601-608.
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10
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0029821726
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A strategy of exon shuffling for making large peptide repertoires displayed on filamentous bacteriophage
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Fisch I, Kontermann RE, Finnern R, Hartley O, Soler-Gonzalez AS, Griffiths AD, Winter G. A strategy of exon shuffling for making large peptide repertoires displayed on filamentous bacteriophage. Proc Natl Acad Sci USA. 93:1996;7761-7766.
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11
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0029001752
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Searching sequence space. Using recombination to search more efficiently and thoroughly instead of making bigger combinatorial libraries
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Stemmer WPC. Searching sequence space. Using recombination to search more efficiently and thoroughly instead of making bigger combinatorial libraries. Bio-Technology. 13:1995;549-553.
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Stemmer, W.P.C.1
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Mimicking somatic hypermutation: Affinity maturation of antibodies displayed on bacteriophage using a bacterial mutator strain
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Low NM, Holliger P, Winter G. Mimicking somatic hypermutation: affinity maturation of antibodies displayed on bacteriophage using a bacterial mutator strain. J Mol Biol. 260:1996;359-368.
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Low, N.M.1
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13
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0028811162
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Phage display selection of ligand residues important for Src homology 3 domain binding specificity
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Rickles RJ, Botfield MC, Zhou X-M, Henry PA, Brugge JS, Zoller MJ. Phage display selection of ligand residues important for Src homology 3 domain binding specificity. Proc Natl Acad Sci USA. 92:1995;10909-10913.
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A combinatorial method for constructing libraries of long peptides displayed by filamentous phage
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Haaparanta T, Huse WD. A combinatorial method for constructing libraries of long peptides displayed by filamentous phage. Mol Div. 1:1995;39-52.
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Yu, J.1
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0028899525
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Phage libraries displaying cyclic peptides with different ring sizes: Ligand specificities of the RGD-directed integrins
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Koivunen E, Wang B, Ruoslahti E. Phage libraries displaying cyclic peptides with different ring sizes: ligand specificities of the RGD-directed integrins. Bio-Technology. 13:1995;265-270.
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Koivunen, E.1
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17
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0029120428
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A peptide isolation from phage display libraries is a structural and functional mimic of an RGD-binding site on integrins
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Pasqualini R, Koivunen E, Ruoslahti E. A peptide isolation from phage display libraries is a structural and functional mimic of an RGD-binding site on integrins. J Cell Biol. 130:1995;1189-1196.
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Pasqualini, R.1
Koivunen, E.2
Ruoslahti, E.3
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18
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0029096892
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Protein ligands of the human adenovirus type 2 outer capsid identified by biopanning of a phage-displayed peptide library on separate domains of wild-type and mutant penton capsomers
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Hong SS, Boulanger P. Protein ligands of the human adenovirus type 2 outer capsid identified by biopanning of a phage-displayed peptide library on separate domains of wild-type and mutant penton capsomers. EMBO J. 14:1995;4714-4727.
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Hong, S.S.1
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19
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Localization of an Arg - Gly - Asp recognition site within an integrin adhesion receptor
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20
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0029117085
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Mapping sites of interaction of p47-phox and flavocytochrome b with random-sequence peptide phage display libraries
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DeLeo FR, Yu L, Burritt JB, Loetterle LR, Bond CW, Jesaitis AJ, Quinn MT. Mapping sites of interaction of p47-phox and flavocytochrome b with random-sequence peptide phage display libraries. Proc Natl Acad Sci USA. 92:1995;7110-7114.
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DeLeo, F.R.1
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21
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9444236174
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Small peptides as potent mimetics of the protein hormone erythropoietin
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of outstanding interest. This paper describes the discovery of a 14-mer peptide capable of mimicking the biological properties of erythropoietin. This demonstrates the feasibility of substituting polypeptide hormones with small molecular weight synthetic compounds, thus opening up a new field of important applications.
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Wrighton NC, Farrell FX, Chang R, Kashyap AK, Barbone FP, Mulcahy LS, Johnson DL, Barrett RW, Jolliffe LK, Dower WJ. Small peptides as potent mimetics of the protein hormone erythropoietin. of outstanding interest Science. 273:1996;458-463 This paper describes the discovery of a 14-mer peptide capable of mimicking the biological properties of erythropoietin. This demonstrates the feasibility of substituting polypeptide hormones with small molecular weight synthetic compounds, thus opening up a new field of important applications.
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Wrighton, N.C.1
Farrell, F.X.2
Chang, R.3
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Mulcahy, L.S.6
Johnson, D.L.7
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Jolliffe, L.K.9
Dower, W.J.10
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22
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0029798402
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Functional mimicry of a protein hormone by a peptide agonist: The EPO receptor complex at 2.8 Å
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Livnah O, Stura EA, Johnson DL, Middleton SA, Mulcahy LS, Wrighton NC, Dower WJ, Jolliffe LK, Wilson IA. Functional mimicry of a protein hormone by a peptide agonist: the EPO receptor complex at 2.8 Å Science. 273:1996;464-471.
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Livnah, O.1
Stura, E.A.2
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Mulcahy, L.S.5
Wrighton, N.C.6
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Wilson, I.A.9
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23
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0026598960
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Human growth hormone and extracellular domain of its receptor: Crystal structure of the complex
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24
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0029670478
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Identification of D-peptide ligand through mirror-image phage display
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Schumacher TNM, Mayr LM, Minor DL Jr, Milhollen MA, Burgess MW, Kim PS. Identification of D-peptide ligand through mirror-image phage display. Science. 271:1996;1854-1857.
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Schumacher, T.N.M.1
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25
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0029947995
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Selection of antigenic and immunogenic mimics of hepatitis C virus using sera from patients
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Prezzi C, Nuzzo M, Meola A, Delmastro P, Galfrè G, Cortese R, Nicosia A, Monaci P. Selection of antigenic and immunogenic mimics of hepatitis C virus using sera from patients. J Immunol. 156:1996;4504-4513.
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26
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0030587888
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Non rheumatoid IgM in HCV-associated type II cryoglobulinemia recognise mimotopes of the CD4-like LAG-3 protein
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Mecchia M, Casato M, Tafi R, Filocamo G, Bonomo L, Fiorilli M, Cortese R, Migliaccio G, Nicosia A. Non rheumatoid IgM in HCV-associated type II cryoglobulinemia recognise mimotopes of the CD4-like LAG-3 protein. J Immunol. 1996;. in press.
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27
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28
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0030158835
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Selection of phage-displayed peptides mimicking Type 1 diabetes-specific epitopes
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Mennuni C, Santini C, Dotta F, Farilla L, DiMario U, Fierabracci A, Bottazzo G, Cortese R, Luzzago A. Selection of phage-displayed peptides mimicking Type 1 diabetes-specific epitopes. J Autoimmun. 9:1996;431-436.
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29
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0011891838
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A novel approach to the aetiopathogenesis of human autoimmune diseases: The use of random peptide phage libraries in the search for disease-related epitopes
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Fierabracci A, Biro PA, Yiangou Y, Mennuni C, Luzzago A, Cortese R, Bottazzo GF. A novel approach to the aetiopathogenesis of human autoimmune diseases: the use of random peptide phage libraries in the search for disease-related epitopes. J Immunol. 1996;. in press.
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Fierabracci, A.1
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30
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0029763438
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Identification of peptides specific for CSF antibodies in multiple sclerosis using phage libraries
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Cortese I, Tafi R, Grimaldi LME, Martino G, Nicosia A, Cortese R. Identification of peptides specific for CSF antibodies in multiple sclerosis using phage libraries. Proc Natl Acad Sci USA. 1996;. in press.
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Cortese, I.1
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31
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Scanning whole cells with phage-display libraries: Identification of peptide ligands that modulate cell function
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Toward cell-targeting gene therapy vectors: Selection of cell-binding peptides from random peptide-presenting phage libraries
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Barry MA, Dower WJ, Johnston SA. Toward cell-targeting gene therapy vectors: selection of cell-binding peptides from random peptide-presenting phage libraries. Nat Med. 2:1996;299-305.
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Barry, M.A.1
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33
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0029932458
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Organ targeting in vivo using phage display peptide libraries
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of special interest. This paper describes a very original method of ligand selection. The RPL is injected as a phage suspension into a living organism and allowed to circulate in the bloodstream. In this way, phage displaying peptides with affinity for certain districts of the body are isolated. With further refinements, this technique might lead to the identification of peptides important for cancer therapy.
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Pasqualini R, Ruoslahti E. Organ targeting in vivo using phage display peptide libraries. of special interest Nature. 380:1996;364-366 This paper describes a very original method of ligand selection. The RPL is injected as a phage suspension into a living organism and allowed to circulate in the bloodstream. In this way, phage displaying peptides with affinity for certain districts of the body are isolated. With further refinements, this technique might lead to the identification of peptides important for cancer therapy.
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Pasqualini, R.1
Ruoslahti, E.2
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34
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0028942281
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Surface expression and ligand-based selection of cDNAs fused to filamentous phage gene VI
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Jespers LS, Messens JH, De Keyser A, Eeckhout D, Van den Brande I, Gansemans YG, Lauwereys MJ, Vlasuk GP, Stanssens PE. Surface expression and ligand-based selection of cDNAs fused to filamentous phage gene VI. Bio-Technology. 13:1995;378-382.
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Jespers, L.S.1
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De Keyser, A.3
Eeckhout, D.4
Van Den Brande, I.5
Gansemans, Y.G.6
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Vlasuk, G.P.8
Stanssens, P.E.9
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Display of peptides and proteins on the surface of bacteriophage λ
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Sternberg N, Hoess RH. Display of peptides and proteins on the surface of bacteriophage λ Proc Natl Acad Sci USA. 92:1995;1609-1613.
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Lindqvist BH, Naderi S. Peptide presentation by bacteriophage P4. FEMS Microbiol Rev. 17:1995;33-39.
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Malarial epitopes expressed on the surface of recombinant tobacco mosaic virus
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Turpen TH, Reinl SJ, Charoenvit Y, Hoffman SL, Fallarme V, Grill LK. Malarial epitopes expressed on the surface of recombinant tobacco mosaic virus. Bio-Technology. 13:1995;53-57.
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40
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0028940472
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Chimeras from a human rhinovirus 14-human immunodeficiency virus type 1 (HIV-1) V3 loop seroprevalence library induce neutralizing responses against HIV-1
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Resnick DA, Smith AD, Geisler SC, Zhang A, Arnold E, Arnold GF. Chimeras from a human rhinovirus 14-human immunodeficiency virus type 1 (HIV-1) V3 loop seroprevalence library induce neutralizing responses against HIV-1. J Virol. 69:1995;2406-2411.
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Resnick, D.A.1
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41
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Eukaryotic virus display: Engineering the major surface glycoprotein of the Autographa californica nuclear polyhedrosis virus (AcNPV) for the presentation of foreign proteins on the virus surface
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Boublik Y, Di Bonito P, Jones IM. Eukaryotic virus display: engineering the major surface glycoprotein of the Autographa californica nuclear polyhedrosis virus (AcNPV) for the presentation of foreign proteins on the virus surface. Bio-Technology. 13:1995;1079-1084.
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Boublik, Y.1
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Jones, I.M.3
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