Abstract
| Original language | English |
|---|---|
| Pages (from-to) | 1113 - 1120 |
| Number of pages | 8 |
| Journal | Nature Biotechnology |
| Volume | 32 |
| Issue number | 11 |
| DOIs | |
| Publication status | Published - 2014 |
Cite this
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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 journal › Article › Research › peer-review
TY - JOUR
T1 - Allosteric targeting of receptor tyrosine kinases
AU - De Smet, Frederik
AU - Christopoulos, Arthur
AU - Carmeliet, Peter
PY - 2014
Y1 - 2014
N2 - 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.
AB - 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.
UR - http://www.nature.com/nbt/journal/v32/n11/pdf/nbt.3028.pdf
U2 - 10.1038/nbt.3028
DO - 10.1038/nbt.3028
M3 - Article
VL - 32
SP - 1113
EP - 1120
JO - Nature Biotechnology
JF - Nature Biotechnology
SN - 1087-0156
IS - 11
ER -