Allosteric targeting of receptor tyrosine kinases

Frederik De Smet, Arthur Christopoulos, Peter Carmeliet

Research output: Contribution to journalArticleResearchpeer-review

68 Citations (Scopus)


The drug discovery landscape has been transformed over the past decade by the discovery of allosteric modulators of all major mammalian receptor superfamilies. Allosteric ligands are a rich potential source of drugs and drug targets with clear therapeutic advantages. G protein?coupled receptors, ligand-gated ion channels and intracellular nuclear hormone receptors have all been targeted by allosteric modulators. More recently, a receptor tyrosine kinase (RTK) has been targeted by an extracellular small-molecule allosteric modulator. Allosteric mechanisms of structurally distinct molecules that target the various receptor families are more alike than originally anticipated and include selectivity, orthosteric probe dependence and pathway-biased signaling.
Original languageEnglish
Pages (from-to)1113 - 1120
Number of pages8
JournalNature Biotechnology
Issue number11
Publication statusPublished - 2014

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