Human antibodies by design
- 1 June 1998
- journal article
- review article
- Published by Springer Nature in Nature Biotechnology
- Vol. 16 (6) , 535-539
- https://doi.org/10.1038/nbt0698-535
Abstract
Monoclonal antibodies (Mabs) have long been considered a good class of natural drugs, both because they mimic their natural role in the body and because they have no inherent toxicity. Although rodent Mabs are readily generated, their widespread use as therapeutic agents has been hampered because they are recognized as foreign by the patient. Evidently, clinical Mabs should be as human as possible and results with some of the more recently developed chimerized and humanized Mabs are testimony to this. Mabs that are entirely human are now being produced from phage display and transgenic mice. The first fully human Mabs generated by phage display have already entered clinical trials, and together with recent advances in these technologies, may finally realize the full potential of antibodies.Keywords
This publication has 50 references indexed in Scilit:
- Isolation of Human Anti-Red Blood Cell Antibodies by Repertoire CloningaAnnals of the New York Academy of Sciences, 2008
- Direct demonstration of MuSK involvement in acetylcholine receptor clustering through identification of agonist ScFvNature Biotechnology, 1997
- Assembly and extension of yeast artificial chromosomes to build up a large locusGene, 1996
- Isolation of Picomolar Affinity Anti-c-erbB-2 Single-chain Fv by Molecular Evolution of the Complementarity Determining Regions in the Center of the Antibody Binding SiteJournal of Molecular Biology, 1996
- Human Antibodies with Sub-nanomolar Affinities Isolated from a Large Non-immunized Phage Display LibraryNature Biotechnology, 1996
- Affinity Maturation of a High-affinity Human Monoclonal Antibody Against the Third Hypervariable Loop of Human Immunodeficiency Virus: Use of Phage Display to Improve Affinity and Broaden Strain ReactivityJournal of Molecular Biology, 1996
- CDR Walking Mutagenesis for the Affinity Maturation of a Potent Human Anti-HIV-1 Antibody into the Picomolar RangeJournal of Molecular Biology, 1995
- Antibody framework residues affecting the conformation of the hypervariable loopsJournal of Molecular Biology, 1992
- Phage antibodies: filamentous phage displaying antibody variable domainsNature, 1990
- Replacing the complementarity-determining regions in a human antibody with those from a mouseNature, 1986