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      Opportunities for therapeutic antibodies directed at G-protein-coupled receptors

      , , ,
      Nature Reviews Drug Discovery
      Springer Nature

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          Abstract

          G protein-coupled receptors (GPCRs) are key drug targets. In this article, Marshall and colleagues discuss the progress made towards generating GPCR-targeting antibodies, including which antigen formats and antibody platforms have been most successful. They review the current pipeline and outline outstanding challenges in antibody generation.

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          Most cited references248

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          Continuous cultures of fused cells secreting antibody of predefined specificity.

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            A comprehensive map of molecular drug targets

            The success of mechanism-based drug discovery depends on the definition of the drug target. This definition becomes even more important as we try to link drug response to genetic variation, understand stratified clinical efficacy and safety, rationalize the differences between drugs in the same therapeutic
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              Strategies and challenges for the next generation of antibody–drug conjugates

              Antibody–drug conjugate (ADCs), which aim to target highly cytotoxic drugs specifically to cancer cells, are one of the fastest growing classes of anticancer therapeutics, with more than 50 such agents currently in clinical trials. This Review discusses lessons learned and emerging strategies in the development of ADCs, including aspects such as target selection, the development of warheads, the optimization of linkers and new conjugation chemistries, and provides an overview of agents that are currently in clinical trials.
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                Author and article information

                Journal
                Nature Reviews Drug Discovery
                Nat Rev Drug Discov
                Springer Nature
                1474-1776
                1474-1784
                July 14 2017
                July 14 2017
                :
                :
                Article
                10.1038/nrd.2017.91
                28860586
                f3536bad-b161-4c1c-88ac-9dd665a1b92c
                © 2017
                History

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