Journal ArticleDOI
By-passing immunisation. Human antibodies from synthetic repertoires of germline VH gene segments rearranged in vitro.
Hennie R. Hoogenboom,Greg Winter +1 more
TLDR
In this article, a repertoire of human VH genes from 49 human germline VH gene segments was rearranged in vitro to create a synthetic third complementarity determining region (CDR) of five or eight residues.About:
This article is published in Journal of Molecular Biology.The article was published on 1992-09-20. It has received 1029 citations till now. The article focuses on the topics: Phage display & Hapten.read more
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Production of chimeric antibodies - a combinatorial approach
Hendricus Renerus Jacobus Matteus Hoogenboom,Michael Baier,Laurent Stephane Anne Therese Jespers,Gregory Paul Winter +3 more
TL;DR: In this paper, the authors describe methods for the production of antibodies, or antibody fragments, which have the same binding specificity as a parent antibody, but which have increased human characteristics.
Journal ArticleDOI
Isolation of high affinity human antibodies directly from large synthetic repertoires.
Andrew D. Griffiths,S C Williams,Oliver Hartley,I M Tomlinson,Peter M. Waterhouse,William L. Crosby,Roland E. Kontermann,Peter T. Jones,N. M. Low,T. J. Allison +9 more
TL;DR: This work created highly diverse repertoires of heavy and light chains entirely in vitro from a bank of human V gene segments and generated a large synthetic repertoire of Fab fragments displayed on filamentous phage to help dissect the contributions of biological mechanisms and structural features governing V gene usage in vivo.
Journal ArticleDOI
Fully synthetic human combinatorial antibody libraries (HuCAL) based on modular consensus frameworks and CDRs randomized with trinucleotides.
Achim Knappik,Liming Ge,Annemarie Honegger,Peter Pack,Melanie Fischer,Günter Wellnhofer,Adolf Hoess,Joachim Wölle,Andreas Plückthun,Bernhard Virnekäs +9 more
TL;DR: The small number of 49 master genes will allow future improvements to be incorporated quickly, and the separation of the frameworks may help in analyzing why nature has evolved these distinct subfamilies of antibody germline genes.
Journal ArticleDOI
Domain antibodies: proteins for therapy
TL;DR: Domain Antibels (dAbs) as discussed by the authors are the smallest known antigen-binding fragments of antibodies, ranging from 11 kDa to 15 kDa, and they are the robust variable regions of the heavy and light chains of immunoglobulins (VH and VL respectively).
Journal ArticleDOI
Selecting and screening recombinant antibody libraries
TL;DR: The first antibody of this new generation, adalimumab (Humira, a human IgG1 specific for human tumor necrosis factor (TNF)), already approved for therapy and with many more in clinical trials, these recombinant antibody technologies will provide a solid basis for the discovery of antibody-based biopharmaceuticals, diagnostics and research reagents for decades to come.
References
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Journal ArticleDOI
DNA sequencing with chain-terminating inhibitors
TL;DR: A new method for determining nucleotide sequences in DNA is described, which makes use of the 2',3'-dideoxy and arabinon nucleoside analogues of the normal deoxynucleoside triphosphates, which act as specific chain-terminating inhibitors of DNA polymerase.
Journal ArticleDOI
Primer-directed enzymatic amplification of DNA with a thermostable DNA polymerase
Randall Keichi Saiki,David H. Gelfand,Susanne Stoffel,Stephen J. Scharf,Russell Higuchi,Glenn Thomas Horn,Kary B. Mullis,Henry A. Erlich +7 more
TL;DR: A thermostable DNA polymerase was used in an in vitro DNA amplification procedure, the polymerase chain reaction, which significantly improves the specificity, yield, sensitivity, and length of products that can be amplified.
Journal ArticleDOI
Phage antibodies: filamentous phage displaying antibody variable domains
TL;DR: It is shown that complete antibody V domains can be displayed on the surface of fd bacteriophage, that the phage bind specifically to antigen and that rare phage can be isolated after affinity chromatography.
Journal ArticleDOI
Replacing the complementarity-determining regions in a human antibody with those from a mouse
TL;DR: This work substituted the CDRs from the heavy-chain variable region of mouse antibody B1–8, which binds the hapten NP-cap, for the corresponding CDRs of a human myeloma protein, to determine whether the antigen-binding site could be transplanted from one framework to another by grafting theCDRs.
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