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Analysis of binding interactions in an idiotope-antiidiotope protein-protein complex by double mutant cycles
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of special interest. Mutational analysis of an idiotope-anti-idiotope complex demonstrated that most of the contact residues make a significant contribution to the energetics of binding. Double mutant analysis was used to quantitate the strength of hydrogen bonds and van der Waal's contacts, as well as probe the context dependence of these different interactions.
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Goldman ER, Dall'Acqua W, Braden BC, Mariuzza RA. Analysis of binding interactions in an idiotope-antiidiotope protein-protein complex by double mutant cycles. of special interest Biochemistry. 36:1997;49-56 Mutational analysis of an idiotope-anti-idiotope complex demonstrated that most of the contact residues make a significant contribution to the energetics of binding. Double mutant analysis was used to quantitate the strength of hydrogen bonds and van der Waal's contacts, as well as probe the context dependence of these different interactions.
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Goldman, E.R.1
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Muller, Y.A.1
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0031571157
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Antibody fragment Fv4155 bound to two closely related steroid hormones: The structural basis of fine specificity
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of special interest. An elegant structural study that suggests a molecular basis for the fine specificity of an antibody fragment binding to two closely related steroids.
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Trinh CH, Hemmington SD, Verhoeyen ME, Phillips SEV. Antibody fragment Fv4155 bound to two closely related steroid hormones: the structural basis of fine specificity. of special interest Structure. 5:1997;937-948 An elegant structural study that suggests a molecular basis for the fine specificity of an antibody fragment binding to two closely related steroids.
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Trinh, C.H.1
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0030993418
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Antibody humanization using monovalent phage display
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of special interest. A humanized antibody fragment was displayed on a phage and the framework region (FR) residues that were known to be important for the CDR conformation were partially randomized. A variant with a 125-fold enhancement in its antigen-binding affinity was isolated from the resulting library. This method is anticipated to be broadly applicable for the optimization of FR residues in humanized antibodies.
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Baca M, Presta L, O'Connor SJ, Wells JA. Antibody humanization using monovalent phage display. of special interest J Biol Chem. 272:1997;10678-10684 A humanized antibody fragment was displayed on a phage and the framework region (FR) residues that were known to be important for the CDR conformation were partially randomized. A variant with a 125-fold enhancement in its antigen-binding affinity was isolated from the resulting library. This method is anticipated to be broadly applicable for the optimization of FR residues in humanized antibodies.
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Baca, M.1
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of special interest. A structural comparison was carried out between murine and humanized versions of an antibody bound to antigen. The grafted murine CDR loops can apparently reconfigure the human framework region (FR) into a conformation that is more like the murine FR. This self-correcting mechanism may have contributed, in part, to the wide success of humanization.
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Holmes MA, Buss TN, Foote J. Conformational correction mechanisms aiding antigen recognition by a humanized antibody. of special interest J Exp Med. 187:1998;479-485 A structural comparison was carried out between murine and humanized versions of an antibody bound to antigen. The grafted murine CDR loops can apparently reconfigure the human framework region (FR) into a conformation that is more like the murine FR. This self-correcting mechanism may have contributed, in part, to the wide success of humanization.
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Holmes, M.A.1
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H domain rotations in engineered antibodies: Crystal structures of the Fab fragments from two murine antitumor antibodies and their engineered human constructs
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H domain rotations in engineered antibodies: crystal structures of the Fab fragments from two murine antitumor antibodies and their engineered human constructs. Proteins. 29:1997;161-171.
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Holliger PT, Prospero T, Winter G. 'Diabodies': small bivalent and bispecific antibody fragments. Proc Natl Acad Sci USA. 90:1993;6444-6448.
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of outstanding interest. A bispecific diabody that binds IgG was demonstrated to support antibody secondary immune functions and have a significantly extended half-life in vivo. This work on endowing a diabody with IgG-like properties, together with the companion study on complement recruitment [30], expands the potential scope of diabodies for human therapy.
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Holliger P, Wing M, Pound JD, Bohlen H, Winter G. Retargeting serum immunoglobulin with bispecific diabodies. of outstanding interest Nat Biotechnol. 15:1997;632-636 A bispecific diabody that binds IgG was demonstrated to support antibody secondary immune functions and have a significantly extended half-life in vivo. This work on endowing a diabody with IgG-like properties, together with the companion study on complement recruitment [30], expands the potential scope of diabodies for human therapy.
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Holliger, P.1
Wing, M.2
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0030743802
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Complement recruitment using bispecific diabodies
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of special interest. A bispecific diabody that binds C1q is shown to direct complement-mediated lysis of sheep red blood cells decorated with the second antigen.
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Kontermann RE, Wing MG, Winter G. Complement recruitment using bispecific diabodies. of special interest Nat Biotechnol. 15:1997;629-631 A bispecific diabody that binds C1q is shown to direct complement-mediated lysis of sheep red blood cells decorated with the second antigen.
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Kontermann, R.E.1
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Single-chain Fv fragments of anti-neuraminidase antibody NC10 containing five- and ten-residue linkers form dimers and with zero-residue linker a trimer
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L, are shown to form noncovalent trimers (called 'triabodies' in the companion paper, [32]) with three functional antigen-binding sites. The high apparent affinity of these trimers, resulting from their multivalency, together with their small size (~ 72 kDa), make them attractive candidates for radio-immuno-imaging and radio-immunotherapy.
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L, are shown to form noncovalent trimers (called 'triabodies' in the companion paper, [32]) with three functional antigen-binding sites. The high apparent affinity of these trimers, resulting from their multivalency, together with their small size (~ 72 kDa), make them attractive candidates for radio-immuno-imaging and radio-immunotherapy.
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Kortt, A.A.1
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L partner. This is a hitherto unknown source of structural and, presumably, functional diversity in the antigen-binding sites of antibodies.
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L partner. This is a hitherto unknown source of structural and, presumably, functional diversity in the antigen-binding sites of antibodies.
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36
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H3 domains that promote the formation of stable heterodimers. Phage optimization provides a complementary and more comprehensive strategy for the rational design [35] and engineering of protein homodimers for heterodimerization.
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H3 domains that promote the formation of stable heterodimers. Phage optimization provides a complementary and more comprehensive strategy for the rational design [35] and engineering of protein homodimers for heterodimerization.
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0001375358
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H. Hoogenboom, J. McCafferty, Chiswell D. Oxford: IRL Press
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Carter P, Rodrigues ML, Park JW, Zapata G. Preparation and uses of Fab' fragments from Escherichia coli. Hoogenboom H, McCafferty J, Chiswell D. Antibody Engineering: a Practical Approach. 1996;291-308 IRL Press, Oxford.
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Carter, P.1
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Delineation of the amino acid residues involved in transcytosis and catabolism of mouse IgG1
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Medesan C, Matesoi D, Radu C, Ghetie V, Ward ES. Delineation of the amino acid residues involved in transcytosis and catabolism of mouse IgG1. J Immunol. 158:1997;2211-2217.
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Medesan, C.1
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40
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0030796064
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Increasing the serum persistence of an IgG fragment by random mutagenesis
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1 Fc were randomized and selected by phage display for binding to the neonatal Fc receptor, FcRn. Two mutant Fc molecules were identified that show higher affinity FcRn binding and a longer in vivo half-life than the wild-type Fc. This study demonstrates a role for FcRn in IgG homeostasis, as well as providing a strategy for manipulating the pharmacokinetic properties of IgG for clinical applications.
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1 Fc were randomized and selected by phage display for binding to the neonatal Fc receptor, FcRn. Two mutant Fc molecules were identified that show higher affinity FcRn binding and a longer in vivo half-life than the wild-type Fc. This study demonstrates a role for FcRn in IgG homeostasis, as well as providing a strategy for manipulating the pharmacokinetic properties of IgG for clinical applications.
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Ghetie, V.1
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H: consequences for thermodynamic stability and folding. J Mol Biol. 265:1997;161-172.
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Antibody scFv fragments without disulfide bonds made by molecular evolution
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of special interest. Site-directed mutagenesis and DNA shuffling were combined with phage display in order to identify mutations that stabilize a scFv molecule lacking disulfide bonds. Such disulfide-free scFv are attractive for intracellular applications where the redox environment is problematic for disulfide-bond formation.
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Proba K, Worn A, Honneger A, Plückthun A. Antibody scFv fragments without disulfide bonds made by molecular evolution. of special interest J Mol Biol. 275:1998;245-253 Site-directed mutagenesis and DNA shuffling were combined with phage display in order to identify mutations that stabilize a scFv molecule lacking disulfide bonds. Such disulfide-free scFv are attractive for intracellular applications where the redox environment is problematic for disulfide-bond formation.
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Proba, K.1
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The rational construction of an antibody against cystatin: Lessons from the crystal structure of an artificial Fab fragment
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Schiweck W, Skerra A. The rational construction of an antibody against cystatin: lessons from the crystal structure of an artificial Fab fragment. J Mol Biol. 268:1997;934-951.
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High level Escherichia coli expression and production of a bivalent humanized antibody fragment
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Carter P, Kelley RF, Rodrigues ML, Snedecor B, Covarrubias M, Velligan MD, Wong WL, Rowland AM, Kotts CE, Carver ME, et al. High level Escherichia coli expression and production of a bivalent humanized antibody fragment. Bio/Technology. 10:1992;163-167.
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Carter, P.1
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Improving in vivo folding and stability of a single-chain Fv antibody fragment by loop grafting
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Jung S, Plückthun A. Improving in vivo folding and stability of a single-chain Fv antibody fragment by loop grafting. Protein Eng. 10:1997;959-966.
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Jung, S.1
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Phage display of a catalytic antibody to optimize affinity for transition-state analog binding
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Baca M, Scanlan TS, Stephenson RC, Wells JA. Phage display of a catalytic antibody to optimize affinity for transition-state analog binding. Proc Natl Acad Sci USA. 94:1997;10063-10068.
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Baca, M.1
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Knappik A, Plückthun A. Engineered turns of a recombinant antibody improve its in vivo folding. Protein Eng. 8:1995;81-89.
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Use of mutator cells as a means for increasing production levels of a recombinant antibody directed against Hepatitis B
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of special interest. The authors demonstrate a 10-fold increase in the apparent production levels of a scFv molecule by selection from a phage display library. This is one of the most promising methods for enhancing antibody fragment expression in E. coli. It is probably generally applicable and can be used in conjunction with the numerous available methods for diversifying phage libraries.
-
Coia G, Ayres A, Lilley GG, Hudson PJ, Irving RA. Use of mutator cells as a means for increasing production levels of a recombinant antibody directed against Hepatitis B. of special interest Gene. 201:1997;203-209 The authors demonstrate a 10-fold increase in the apparent production levels of a scFv molecule by selection from a phage display library. This is one of the most promising methods for enhancing antibody fragment expression in E. coli. It is probably generally applicable and can be used in conjunction with the numerous available methods for diversifying phage libraries.
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(1997)
Gene
, vol.201
, pp. 203-209
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Coia, G.1
Ayres, A.2
Lilley, G.G.3
Hudson, P.J.4
Irving, R.A.5
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52
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0029955258
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Selection of linkers for a catalytic single-chain antibody using phage display technology
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Tang Y, Jiang N, Parakh C, Hilvert D. Selection of linkers for a catalytic single-chain antibody using phage display technology. J Biol Chem. 271:1996;15682-15686.
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(1996)
J Biol Chem
, vol.271
, pp. 15682-15686
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Tang, Y.1
Jiang, N.2
Parakh, C.3
Hilvert, D.4
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53
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0031584314
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Importance of the linker in expression of single-chain Fv antibody fragments: Optimisation of peptide sequence using phage display technology
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Turner DJ, Ritter MA, George AJ. Importance of the linker in expression of single-chain Fv antibody fragments: optimisation of peptide sequence using phage display technology. J Immunol Methods. 205:1997;43-54.
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(1997)
J Immunol Methods
, vol.205
, pp. 43-54
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Turner, D.J.1
Ritter, M.A.2
George, A.J.3
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54
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0030965970
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Disrupting the hydrophobic patches at the antibody variable/constant domain interface: Improved in vivo folding and physical characterization of an engineered scFv fragment
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Nieba L, Honneger A, Krebber C, Plückthun A. Disrupting the hydrophobic patches at the antibody variable/constant domain interface: improved in vivo folding and physical characterization of an engineered scFv fragment. Protein Eng. 10:1997;435-444.
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(1997)
Protein Eng
, vol.10
, pp. 435-444
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Nieba, L.1
Honneger, A.2
Krebber, C.3
Plückthun, A.4
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55
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0031029555
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In vitro scanning mutagenesis of an antibody binding pocket
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of outstanding interest. The very rapid mutational analysis of an antibody is demonstrated using in vitro transcription and translation to circumvent time-consuming cloning and in vivo expression steps. This is a generic technology that is applicable to other proteins.
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Burks EA, Chen G, Georgiou G, Iverson BL. In vitro scanning mutagenesis of an antibody binding pocket. of outstanding interest Proc Natl Acad Sci USA. 94:1997;412-417 The very rapid mutational analysis of an antibody is demonstrated using in vitro transcription and translation to circumvent time-consuming cloning and in vivo expression steps. This is a generic technology that is applicable to other proteins.
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(1997)
Proc Natl Acad Sci USA
, vol.94
, pp. 412-417
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Burks, E.A.1
Chen, G.2
Georgiou, G.3
Iverson, B.L.4
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56
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0031021109
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Functional antibody production using cell-free translation: Effects of protein disulfide isomerase and chaperones
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of special interest. A thorough study describing the optimization of the production of functional scFv molecules by in vitro transcription and translation.
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Ryabova LA, Desplancq D, Spirin AS, Plückthun A. Functional antibody production using cell-free translation: effects of protein disulfide isomerase and chaperones. of special interest Nat Biotechnol. 15:1997;79-84 A thorough study describing the optimization of the production of functional scFv molecules by in vitro transcription and translation.
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(1997)
Nat Biotechnol
, vol.15
, pp. 79-84
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Ryabova, L.A.1
Desplancq, D.2
Spirin, A.S.3
Plückthun, A.4
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57
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0028291823
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Isolation of high-affinity human antibodies directly from large synthetic repertoires
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Griffiths A, Williams SC, Hartley O, Tomlison IM, Waterhouse P, Crosby WL, Kontermann RE, Jones PT, Low NM, Allison TJ, et al. Isolation of high-affinity human antibodies directly from large synthetic repertoires. EMBO J. 13:1994;3245-3260.
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(1994)
EMBO J
, vol.13
, pp. 3245-3260
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Griffiths, A.1
Williams, S.C.2
Hartley, O.3
Tomlison, I.M.4
Waterhouse, P.5
Crosby, W.L.6
Kontermann, R.E.7
Jones, P.T.8
Low, N.M.9
Allison, T.J.10
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58
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0030803049
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Direct demonstration of MuSK involvement in acetylcholine receptor clustering through identification of agonist scFv
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d < 10 nM). This is a rapid and perhaps general route for generating highly specific agonist antibodies.
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d < 10 nM). This is a rapid and perhaps general route for generating highly specific agonist antibodies.
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(1997)
Nat Biotechnol
, vol.15
, pp. 768-771
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Xie, M.H.1
Yuan, J.2
Adams, C.3
Gurney, A.4
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59
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0032006660
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Increased affinity leads to improved selective tumor delivery of single-chain Fv antibodies
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of outstanding interest. Tumor targeting was undertaken using scFv molecules with varying affinities (320 to 1 nM) for the tumor-associated antigen HER2/neu. The extent and specificity of tumor localization was greatly improved by increasing the antigen-binding affinity.
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Adams GP, Schier R, Marshall K, Wolf EJ, McCall AM, Marks JD, Weiner LM. Increased affinity leads to improved selective tumor delivery of single-chain Fv antibodies. of outstanding interest Cancer Res. 58:1998;485-490 Tumor targeting was undertaken using scFv molecules with varying affinities (320 to 1 nM) for the tumor-associated antigen HER2/neu. The extent and specificity of tumor localization was greatly improved by increasing the antigen-binding affinity.
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(1998)
Cancer Res
, vol.58
, pp. 485-490
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-
Adams, G.P.1
Schier, R.2
Marshall, K.3
Wolf, E.J.4
McCall, A.M.5
Marks, J.D.6
Weiner, L.M.7
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60
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0030700632
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Targeting by affinity-matured recombinant antibody fragments of an angiogenesis associated fibronectin isoform
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of outstanding interest. The targeting of a scFv molecule to the tumor neovasculature-associated antigen oncofetal fibronectin was greatly improved using both affinity-matured and dimeric fragments. Imaging in real time was possible by IR photodetection using a fluorophore that was chemically coupled to the antibody fragment.
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Neri D, Carnemolla B, Nissim A, Leprini A, Querze G, Balza E, Pini A, Tarli L, Halin C, Neri P, et al. Targeting by affinity-matured recombinant antibody fragments of an angiogenesis associated fibronectin isoform. of outstanding interest Nat Biotechnol. 15:1997;1271-1275 The targeting of a scFv molecule to the tumor neovasculature-associated antigen oncofetal fibronectin was greatly improved using both affinity-matured and dimeric fragments. Imaging in real time was possible by IR photodetection using a fluorophore that was chemically coupled to the antibody fragment.
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(1997)
Nat Biotechnol
, vol.15
, pp. 1271-1275
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-
Neri, D.1
Carnemolla, B.2
Nissim, A.3
Leprini, A.4
Querze, G.5
Balza, E.6
Pini, A.7
Tarli, L.8
Halin, C.9
Neri, P.10
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61
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0031560775
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Selectively-infective phage (SIP): A mechanistic dissection of a novel in vivo selection for protein-ligand interactions
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Krebber C, Spada S, Desplancq D, Krebber A, Ge L, Plückthun A. Selectively-infective phage (SIP): a mechanistic dissection of a novel in vivo selection for protein-ligand interactions. J Mol Biol. 268:1997;607-618.
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(1997)
J Mol Biol
, vol.268
, pp. 607-618
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Krebber, C.1
Spada, S.2
Desplancq, D.3
Krebber, A.4
Ge, L.5
Plückthun, A.6
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62
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0030869953
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Affinity and folding properties both influence the selection of antibodies with the selectively infective phage (SIP) methodology
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of special interest. A small and well-characterized library was used for the evaluation of the phage display technology SIP. This method apparently selects for many properties of the displayed molecule, including folding, stability and affinity.
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Pedrazzi G, Schwesinger F, Honneger A, Krebber C, Plückthun A. Affinity and folding properties both influence the selection of antibodies with the selectively infective phage (SIP) methodology. of special interest FEBS Lett. 415:1997;289-293 A small and well-characterized library was used for the evaluation of the phage display technology SIP. This method apparently selects for many properties of the displayed molecule, including folding, stability and affinity.
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(1997)
FEBS Lett
, vol.415
, pp. 289-293
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Pedrazzi, G.1
Schwesinger, F.2
Honneger, A.3
Krebber, C.4
Plückthun, A.5
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63
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0031592934
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Selective phage infection mediated by epitope expression on F pilus
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of special interest. Genetically fusing a peptide to pilin prevents the infection of E. coli by wild-type M13 phages. Infection can be selectively restored by displaying on the phage a specific scFv that is capable of interacting with the pilin-peptide fusion. This work directly provides a foundation for identifying anti-peptide antibodies from scFv libraries.
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Malmborg AC, Soderlind E, Frost L, Borrebaeck CAK. Selective phage infection mediated by epitope expression on F pilus. of special interest J Mol Biol. 273:1997;544-551 Genetically fusing a peptide to pilin prevents the infection of E. coli by wild-type M13 phages. Infection can be selectively restored by displaying on the phage a specific scFv that is capable of interacting with the pilin-peptide fusion. This work directly provides a foundation for identifying anti-peptide antibodies from scFv libraries.
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(1997)
J Mol Biol
, vol.273
, pp. 544-551
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Malmborg, A.C.1
Soderlind, E.2
Frost, L.3
Borrebaeck, C.A.K.4
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64
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0029585566
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Co-selection of cognate antibody-antigen pairs by selectively-infective phages
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Krebber C, Spada S, Desplancq D, Pluckthun A. Co-selection of cognate antibody-antigen pairs by selectively-infective phages. FEBS Lett. 377:1995;227-231.
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(1995)
FEBS Lett
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, pp. 227-231
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Krebber, C.1
Spada, S.2
Desplancq, D.3
Pluckthun, A.4
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65
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0030704683
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Making chemistry selectable by linking it to infectivity
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Gao C, Lin CH, Lo CHL, Mao S, Wirsching P, Lerner RA, Janda KD: Making chemistry selectable by linking it to infectivity. Proc Natl Acad Sci USA 94: 11777-11782.
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Proc Natl Acad Sci USA
, vol.94
, pp. 11777-11782
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Gao, C.1
Lin, C.H.2
Lo, C.H.L.3
Mao, S.4
Wirsching, P.5
Lerner, R.A.6
Janda, K.D.7
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66
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0028592703
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An in vitro polysome display system for identifying ligands from very large peptide libraries
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Mattheakis LC, Bhatt RR, Dower WJ. An in vitro polysome display system for identifying ligands from very large peptide libraries. Proc Natl Acad Sci USA. 91:1994;9022-9026.
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(1994)
Proc Natl Acad Sci USA
, vol.91
, pp. 9022-9026
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Mattheakis, L.C.1
Bhatt, R.R.2
Dower, W.J.3
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67
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0030974119
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In vitro selection and evolution of functional proteins by using ribosome display
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of outstanding interest. This is the first successful demonstration of ribosome display technology using proteins. This method, together with that in [68], is anticipated be generally useful for the identification and molecular evolution of proteins or peptides that bind targets of interest.
-
Hanes J, Plückthun A. In vitro selection and evolution of functional proteins by using ribosome display. of outstanding interest Proc Natl Acad Sci USA. 94:1997;4937-4942 This is the first successful demonstration of ribosome display technology using proteins. This method, together with that in [68], is anticipated be generally useful for the identification and molecular evolution of proteins or peptides that bind targets of interest.
-
(1997)
Proc Natl Acad Sci USA
, vol.94
, pp. 4937-4942
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-
Hanes, J.1
Plückthun, A.2
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68
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0031574037
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Antibody-ribosome-mRNA (ARM) complexes as efficient selection particles for in vitro display and evolution of antibody combining sites
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5-fold were obtained in a single cycle.
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5-fold were obtained in a single cycle.
-
(1997)
Nucleic Acids Res
, vol.25
, pp. 5132-5134
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He, M.1
Taussig, M.J.2
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69
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0031876578
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An efficient route to human bispecific IgG
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of outstanding interest. The production of human bispecific IgG (BsIgG) by co-expressing two different antibodies is inefficient due to unwanted pairings of the component heavy and light chains. A broadly applicable method was developed that overcomes these problems, enabling near quantitative formation and efficient recovery of human BsIgG. This technology substantially expands the clinical potential of human BsIgG.
-
Merchant AM, Zhu Z, Yuan JQ, Goddard A, Adams CW, Presta LG, Carter P. An efficient route to human bispecific IgG. of outstanding interest Nat Biotechnol. 16:1998;677-681 The production of human bispecific IgG (BsIgG) by co-expressing two different antibodies is inefficient due to unwanted pairings of the component heavy and light chains. A broadly applicable method was developed that overcomes these problems, enabling near quantitative formation and efficient recovery of human BsIgG. This technology substantially expands the clinical potential of human BsIgG.
-
(1998)
Nat Biotechnol
, vol.16
, pp. 677-681
-
-
Merchant, A.M.1
Zhu, Z.2
Yuan, J.Q.3
Goddard, A.4
Adams, C.W.5
Presta, L.G.6
Carter, P.7
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