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Post-graduate Certificate in Academic Practice, ºÚÁϳԹÏÍø

PhD Biochemistry, University College London

BSc (Hons) Biomedical Sciences (with placement), University of Wolverhampton

Debbie is Deputy Director of Education for the College of Life and Environmental Sciences with responsibility for assuring the quality of the College’s academic provision. She is also Senior Tutor in Biosciences overseeing the tutorial system and acting as the interface between wellbeing and teaching and learning.

Debbie began her scientific career in the pharmaceutical industry, investigating the pharmacokinetics of novel compounds. She was then awarded a CASE award from the MRC to carry out a collaborative PhD at the National Institute of Medical Research, Mill Hill and GlaxoSmithKline during which she used biophysical techniques to investigate the enzymatic properties of a Rho GTPase-activating protein. Debbie remained at GlaxoSmithKline to carry out her first post-doctoral research position, developing assays to identify inhibitors of protein-protein interactions.

In 2002 Debbie moved to the ºÚÁϳԹÏÍø when she began work as a post-doctoral scientist investigating Fibroblast Growth Factor signalling in cancer and is currently a teaching-focused lecturer within the Structural and Molecular Cell Biology theme in the School of Biosciences.

Cell and Developmental Biology (2nd year undergraduate)

Cancer Biology (3^rd/4th year undergraduate) 

Omics for Biomedical research (3^rd/4th year undergraduate) – module lead

Research Development and Funding (MSci)

In response to extra- and intra- cellular signals, post-translational modifications (PTMs) on proteins can be altered to modulate protein activity, stability, spatial localisation and interaction with other molecules. Phosphorylation is a key PTM involved in the transduction of cell signalling events, and aberrant phosphorylation is linked to human disease. A major focus of Debbie’s research has been to obtain a ‘systems-wide’ understanding of phosphorylation events in signalling networks controlled by fibroblast growth factor receptor (FGFR) and platelet-derived growth factor receptor (PDGFR), two proteins which are often overexpressed in cancer. Mass spectrometry based quantitative proteomic techniques have been used to identify phosphorylation events and protein-protein interactions providing insight into regulation of key signalling networks that are switched on during cancer. The findings have implications for the application of current therapies and the development of new therapies. 

School governor (20-current)

External member of the Programme Approval and Review panel for Open University (23)

Designated Quality Body Assessor for the QAA (22-23) 

Editor for Nature Scientific Reports (18-21) 

Committee member for the East Midlands Proteomics Workshop (EMPW) (15-20)