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- W2642015544 abstract "Structural insights have been revealed from X-ray co-complexes of a range of G protein-coupled receptors (GPCRs) and their allosteric ligands. The understanding of how small molecules can modulate the function of this important class of receptors by binding to a diverse range of pockets on and inside the proteins has had a profound impact on the structure-based drug design (SBDD) of new classes of therapeutic agents. The types of allosteric pockets and the mode of modulation as well as the advantages and disadvantages of targeting allosteric pockets (as opposed to the natural orthosteric site) are considered in the context of these new structural findings." @default.
- W2642015544 created "2017-06-30" @default.
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- W2642015544 date "2017-09-01" @default.
- W2642015544 modified "2023-10-16" @default.
- W2642015544 title "Applying Structure-Based Drug Design Approaches to Allosteric Modulators of GPCRs" @default.
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- W2642015544 doi "https://doi.org/10.1016/j.tips.2017.05.010" @default.
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