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We aim to understand the proteins that transmit signals within the cell and the signalling pathways that regulate the cell’s functions. Understanding these pathways and proteins enables the discovery of new drug targets for treating disease.

Cellular Signalling Group July 2023

Introduction

Key proteins of interest in our research are those that catalyse post-translational modifications such as phosphorylation or ADP-ribosylation. Phosphorylation is catalysed by protein kinases; there are over 500 protein kinases in the human genome and most of them remain poorly characterized despite their importance in regulating physiology. Furthermore, ADP-ribosylation is important in numerous cellular processes such as DNA damage detection and repair as well as metabolism, host-virus interactions and epigenetic regulation. Our approach is to use high resolution structural information for the generation of selective inhibitors (i.e. chemical probes) which we use to gain an understanding of the different functions of kinase proteins. We have therefore generated a large repository of efficient expression systems, recombinant proteins and crystal structures that enable family-wide structural comparison and screening.

In addition to our work on kinases, we have interests in lipid kinases and sphingolipid biosynthesis—both of which have strong links to inflammation and cancer—and where mutations in the proteins involved are associated with a variety of rare diseases.

Our team

Recent publications

Tetrahydropyrazolopyridinones as a Novel Class of Potent and Highly Selective LIMK Inhibitors.

Journal article

Baldwin AG. et al, (2025), J Med Chem, 68, 17427 - 17456

Discovery of MDI-114215: A Potent and Selective LIMK Inhibitor To Treat Fragile X Syndrome.

Journal article

Baldwin AG. et al, (2025), J Med Chem, 68, 719 - 752

Covalent Inhibitors of S100A4 Block the Formation of a Pro-Metastasis Non-Muscle Myosin 2A Complex.

Journal article

Giroud C. et al, (2024), J Med Chem, 67, 18943 - 18956

A ligand discovery toolbox for the WWE domain family of human E3 ligases.

Journal article

Münzker L. et al, (2024), Commun Biol, 7