References
- Annu Rev Biomed Eng. v.2 Antibody engineering Maynard, J.;G. Georgiou https://doi.org/10.1146/annurev.bioeng.2.1.339
- Trends Biotechnol. v.13 Clinical issues in antibody design Chester, K. A.;R. E. Hawkins https://doi.org/10.1016/S0167-7799(00)88968-4
- Nature v.321 Replacing the complementarity-determining regions in a human antibody with those from a mouse Jones, P. T.;P. H. Dear;J. Foote;M. S. Neuberger;G. Winter https://doi.org/10.1038/321522a0
- Nature v.332 Reshaping human antibodies for therapy Riechmann, L.;M. Clark;H. Waldmann;G. G. Winter https://doi.org/10.1038/332323a0
- Mol. Immunol. v.32 The immunogenicity of the 7E3 murine monoclonal Fab antibody fragment variable region is dramatically reduced in humans by substitution of human for murine constant regions Knight, D. M.;C. Wagner;R. Jordan;M. F. McAleer;R. DeRita;D. N. Fass;B. S. Coller;H. F. Weisman;J. Ghrayeb https://doi.org/10.1016/0161-5890(95)00085-2
- Immunol. Rev. v.130 Engineering antibodies for therapy Adair, J. R. https://doi.org/10.1111/j.1600-065X.1992.tb01519.x
- Nature v.363 Naturally occurring antibodies devoid of light chains Hamers-Casterman, C.;T. Atarhouch;S. Muyldermans;G. Robinson;C. Hamers;E. B. Songa;N. Bendahman;R. Hamers https://doi.org/10.1038/363446a0
- Nature Struct. Biol. v.3 Crystal structure of a camel single-domain VH antibody fragment in complex with lysozyme Desmyter, A.;T. R. Transue;M. A. Ghahroudi;M. H. Thi;F. Poortmans;R. Hamers;S. Muyldermans; L. Wyns https://doi.org/10.1038/nsb0996-803
- Structure Fold. Des. v.7 A single-domain antibody fragment in complex with RNase A: Non-canonical loop structures and nanomolar affinity using two CDR loops Decanniere, K.;A. Desmyter;M. Lauwereys;M. A. Ghahroudi;S. Muyldermans;L. Wyns https://doi.org/10.1016/S0969-2126(99)80049-5
- Int. J. Cancer. v.98 Efficient tumor targeting by singledomain antibody fragments of camels Cortez-Retamozo, V.;M. Lauwereys;G. Hassanzadeh Gh;M. Gobert;K. Conrath;S. Muyldermans;P. De Baetselier;H. Revets https://doi.org/10.1002/ijc.10212
- J. Mol. Biol. v.290 An antibody single-domain phage display library of a native heavy chain variable region: isolation of functional single-domain VH molecules with a unique interface Reiter, Y.;P. Schuck;L. F. Boyd;D. Plaksin https://doi.org/10.1006/jmbi.1999.2923
- Proc Natl Acad Sci. v.85 Protein engineering of antibody binding sites: recovery of specific activity in an anti-digoxin single-chain Fv analogue produced in Escherichia coli Huston, J. S.;D. Levinson;M. Mudgett-Hunter;M. S. Tai;J. Movotny;M. N. Margolies;R. J. Ridge;R. E. Bruccoleri;E. Haber;R. Crea https://doi.org/10.1073/pnas.85.16.5879
- Biochemistry v.30 Conformational stability, folding, and ligand-binding affinity of single-chain Fv immunoglobulin fragments expressed in Escherichia coli Pantoliano, M. W.;R. E. Bird;S. Johnson;E. D. Asel;S. W. Dodd;J. F. Wood;K. D. Hardman https://doi.org/10.1021/bi00106a007
- J. Immunol. Methods v.205 Importance of the linker in expression of single-chain Fv antibody fragments: optimisation of peptide sequence using phage display technology Turner, D. J.;M. A. Ritter;A. J. George https://doi.org/10.1016/S0022-1759(97)00057-4
- Proc. Natl. Acad. Sci. v.95 Optimizing the stability of single-chain proteins by linker length and composition mutagenesis Robinson, C. R.;R. T. Sauer https://doi.org/10.1073/pnas.95.11.5929
- Biotechnology v.10 High level Escherichia coli expression and production of a bivalent humanized antibody fragment Carter, P.;R. F. Kelley;M. L. Rodrigues;B. Snedecor;M. Covarrubias;M. D. Velligan;W. L. Wong;A. M. Rowland;C. E. Kotts;M. E. Carver (et al) https://doi.org/10.1038/nbt0292-163
- Nature v.348 Phage antibodies: filamentous phage displaying antibody variable domains McCafferty, J.;A. D. Griffiths;G. Winter;D. J. Chiswell https://doi.org/10.1038/348552a0
- Nucleic Acids Res. v.19 Multi-subunit proteins on the surface of filamentous phage: methodologies for displaying antibody (Fab) heavy and light chains Hoogenboom, H. R.;A. D. Griffiths;K. S. Johnson;D. J. Chiswell;P. Hudson;G. Winter https://doi.org/10.1093/nar/19.15.4133
- Biotechnology v.9 Fab assembly and enrichment in a monovalent phage display system Garrard, L. J.;M. Yang;M. P. O'Connell;R. F. Kelley;D. J. Henner https://doi.org/10.1038/nbt1291-1373
- J. Immunol. v.147 Expression of antibody Fab domains on bacteriophage surfaces. Potential use for antibody selection Chang, C. N.;N. F. Landolfi;C. Queen
- Nature Biotechnol. v.14 Phage diabody repertoires for selection of large numbers of bispecific antibody fragments McGuinness, B. T.;G. Walter;K. FitzGerald;P. Schuler;W. Mahoney;A. R. Duncan;H. R. Hoogenboom https://doi.org/10.1038/nbt0996-1149
- Curr. Opin. Biotechnol. v.11 The use of recombinant antibodies in proteomics Holt, L. J.;C. Enever;R. M. de Wildt;I. M. Tomlinson https://doi.org/10.1016/S0958-1669(00)00133-6
- J. Mol. Biol. v.296 Fully synthetic human combinatorial antibody libraries (HuCAL) based on modular consensus frameworks and CDRs randomized with trinucleotides Knappik, A.;L. Ge;A. Honegger;P. Pack;M. Fischer;G.Wellnhofer;A. Hoess;J. Wolle;A. Pluckthun;B. Virnekas
- Nature Biotechnol. v.18 Picomolar affinity antibodies from a fully synthetic naive library selected and evolved by ribosome display Hanes, J.;C. Schaffitzel;A. Knappik;A. Pluckthun https://doi.org/10.1038/82407
- In IBC International Conference on Antibody Engineering
- Nature Biotechnol. v.14 High-avidity human IgG kappa monoclonal antibodies from a novel strain of minilocus transgenic mice Fishwild, D. M.;S. L. O'Donnell;T. Bengoechea;D. V. Hudson;F. Harding;S. L. Bernhard;D. Jones;R. M. Kay;K. M. Higgins;S. R. Schramm;N. Lonberg https://doi.org/10.1038/nbt0796-845
- Curr. Opin. Biotechnol. v.8 Production of human antibody repertoires in transgenic mice Bruggemann, M.;M. J. Taussig https://doi.org/10.1016/S0958-1669(97)80068-7
- Trends Biotechnol. v.17 Exploiting antibody-based technologies to manage environmental pollution Harris, B. https://doi.org/10.1016/S0167-7799(99)01308-6
- J. Mol. Biol. v.315 Towards proteome-wide production of monoclonal antibody by phage display Liu, B.;L. Huang;C. Sihlbom;A. Burlingame;J. D. Marks https://doi.org/10.1006/jmbi.2001.5276
- Nature Biotechnol. v.18 Antibody arrays for high-throughput screening of antibody-antigen interactions de Wildt, R. M.;C. R. Mundy;B. D. Gorick;I. M. Tomlinson https://doi.org/10.1038/79494
- Nucleic Acids Res. v.28 By-passing selection: direct screening for antibody-antigen interactions using protein arrays Holt, L. J.;K. Bussow;G. Walter;I. M. Tomlinson https://doi.org/10.1093/nar/28.15.e72