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Structure-Guided Design of Antibodies
Current Computer Aided-Drug Design, 2010Monoclonal antibodies capable of recognizing antigens with high affinity and specificity represent a wellestablished class of biological agents. Since the development of hybridoma technology in 1975, advances in recombinant DNA technologies and computational and biophysical methods have allowed us to develop a better understanding of the relationships ...
Justin A, Caravella +3 more
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Antibody Modeling: Implications for Engineering and Design
Methods, 2000Our understanding of the rules relating sequence to structure in antibodies has led to the development of accurate knowledge-based procedures for antibody modeling. Information gained from the analysis of antibody structures has been successfully exploited to engineer antibody-like molecules endowed with prescribed properties, such as increased ...
Morea V, Lesk, AM, Tramontano, A
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Design of synthetic antibody libraries
Expert Opinion on Biological Therapy, 2007Antibody libraries came into existence 15 years ago when the accumulating sequence data of immunoglobulin genes and the advent of polymerase chain reaction technology made it possible to clone antibody gene repertoires. Since then, virtually hundreds of antibody libraries have been constructed, employing limitless maneuvers from the antibody ...
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Toward aggregation-resistant antibodies by design
Trends in Biotechnology, 2013Monoclonal antibodies are attractive therapeutics for treating a wide range of human disorders due to their exquisite binding specificity and high binding affinity. However, a limitation of antibodies is their highly variable and difficult-to-predict propensities to aggregate when concentrated during purification and delivery.
Christine C, Lee +2 more
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Potent antibody therapeutics by design
Nature Reviews Immunology, 2006Antibodies constitute the most rapidly growing class of human therapeutics and the second largest class of drugs after vaccines. The generation of potent antibody therapeutics, which I review here, is an iterative design process that involves the generation and optimization of antibodies to improve their clinical potential.
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Rational Design of Antibody Protease Inhibitors
Journal of the American Chemical Society, 2015The bovine antibody BLV1H12, which has an ultralong CDR3H, provides a novel scaffold for engineering new functions into the antibody's variable region. By modifying the β-strand "stalk" of BLV1H12 with sequences derived from natural or synthetic protease inhibitors, we have generated antibodies that inhibit bovine trypsin and human neutrophil elastase (
Tao, Liu +7 more
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Antibody design: Beyond the natural limits
Trends in Biotechnology, 1994Dissection of antibody-antigen interactions requires a knowledge of antibody structure, the ability to model accurately the conformation of antibody-combining sites, and an understanding of the energetic factors governing the interactions. When this understanding has reached the point where the molecular shape and chemical character of a combining site
A R, Rees +5 more
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A Novel Monoclonal Antibody Design for Radioimmunotherapy
Cancer Biotherapy and Radiopharmaceuticals, 2003The generation of chimeric and complementary-determining region (CDR) grafted monoclonal antibodies (MAb) have reduced the immunogenicity problem in the clinical application of radioimmunotherapy with monoclonal antibodies. However, humanization (Hu) has prolonged the circulation (plasma T1/2) of radiolabeled antibodies, resulting in an increased ...
Andres, Forero +7 more
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Designing stable humanized antibodies
Nature Biomedical Engineering, 2023Alissa M. Hummer, Charlotte M. Deane
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Antibody Affinity Maturation by Computational Design
2018The immune systems protect our bodies from foreign molecules or antigens, where antibodies play important roles. Antibodies evolve over time upon antigen encounter by somatically mutating their genome sequences. The end result is a series of antibodies that display higher affinities and specificities to specific antigens.
Daisuke, Kuroda, Kouhei, Tsumoto
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