Henry Wellcome Building of Genomic Medicine
|The structure of the RPTPmu trans dimer (Aricescu et al Science 2007)|
|Semaphorin-plexin recognition complex (Janssen et al Nature 2010)|
E. Yvonne Jones
Professor of Protein Crystallography
Yvonne Jones is Director of the Cancer Research UK Receptor Structure Research Group which is focused on the structural biology of extracellular recognition and signalling complexes. The group's core techniques include protein crystallography and, increasingly, cryo electron microscopy, which are used to generate high resolution structural information. Importantly, studies using these techniques are integrated with advanced light microscopy and cryo electron tomography, as well as cell-based functional studies, to probe molecular mechanisms at the cell surface.
The group's research addresses fundamental questions about cell-cell signalling systems of importance to human health. How are signalling assemblies arranged? Which features are necessary for normal signal transduction into the cell? What mechanisms trigger dysfunctional signalling? The work ties into an extensive network of interdisciplinary local and international collaborations with the ultimate aim of learning how to manipulate these signalling systems for the design of new clinical therapies. Current projects within the group focus on signalling systems of importance in developmental biology. These include systems involved in cell guidance (e.g. semaphorin/plexin and ephrin/Eph signalling), as well as mechanisms controlling signalling by the Wnt family of morphogens.
NOTUM from Apc-mutant cells biases clonal competition to initiate cancer.
Flanagan DJ. et al, (2021), Nature
Small-molecule inhibitors of carboxylesterase Notum
Zhao Y. et al, (2021), Future Medicinal Chemistry
Notum Deacylates Octanoylated Ghrelin
Zhao Y. et al, (2021), Molecular Metabolism, 101201 - 101201
A variant in IL6ST with a selective IL-11 signaling defect in human and mouse
Schwerd T. et al, (2020), Bone Research, 8
Caffeine inhibits Notum activity by binding at the catalytic pocket
Zhao Y. et al, (2020), Communications Biology, 3