Allosteric targeting of receptor tyrosine kinases

Frederik De Smet, Arthur Christopoulos, Peter Carmeliet

Research output: Contribution to journalArticleResearchpeer-review

Abstract

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
Volume32
Issue number11
DOIs
Publication statusPublished - 2014

Cite this

De Smet, Frederik ; Christopoulos, Arthur ; Carmeliet, Peter. / Allosteric targeting of receptor tyrosine kinases. In: Nature Biotechnology. 2014 ; Vol. 32, No. 11. pp. 1113 - 1120.
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Allosteric targeting of receptor tyrosine kinases. / De Smet, Frederik; Christopoulos, Arthur; Carmeliet, Peter.

In: Nature Biotechnology, Vol. 32, No. 11, 2014, p. 1113 - 1120.

Research output: Contribution to journalArticleResearchpeer-review

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