I am a Marie Curie IEF Research Fellow in the Department of Chemistry at Imperial College London. For over 5 years the main focus of my research has been the development of chemical tools for studying post-translational modifications of proteins. Since January 2011 I have been engaged in a chemical proteomic project in the Laboratory of Dr Edward Tate in the Department. The project aims to develop and apply novel chemical probes to perform the first direct comparison of protein lipidation (acylation, prenylation, cholesterylation) and lipidation enzymology in aggressive cancer cell lines vs. benign cells in order to identify enzymes and pathways worthy of further investigation as novel drug targets. My previous work includes the discovery of a new bioconjugation method, Staudinger-phosphite ligation, and its utilization to gain an unprecedented spatial and temporal control over the presentation of phosphate groups on proteins that is expected to significantly influence studies on protein phosphorylation/dephosphorylation pathways (Angew. Chem. Int. Ed. 2009, 48, 8234), and the development of novel probes for studying covalent adducts between polyunsaturated fatty acid-derived electrophiles and nucleophilic sites on proteins (Nat. Chem. Biol. 2010, 6, 205).
et al., 2017, Dynamic protein acylation: new substrates, mechanisms and drug targets, Trends in Biochemical Sciences, Vol:42, ISSN:0968-0004, Pages:566-581
et al., 2017, Open Source High Content Analysis Utilizing Automated Fluorescence Lifetime Imaging Microscopy, Jove-journal of Visualized Experiments, ISSN:1940-087X
et al., 2016, Global Profiling of Huntingtin-associated protein E (HYPE)-Mediated AMPylation through a Chemical Proteomic Approach, Molecular & Cellular Proteomics, Vol:15, ISSN:1535-9476, Pages:715-725
Teo CSH, Serwa RA, O'Hare P, 2016, Spatial and Temporal Resolution of Global Protein Synthesis during HSV Infection Using Bioorthogonal Precursors and Click Chemistry, Plos Pathogens, Vol:12, ISSN:1553-7366
et al., 2015, Systems Analysis of Protein Fatty Acylation in Herpes Simplex Virus-Infected Cells Using Chemical Proteomics, Chemistry & Biology, Vol:22, ISSN:1074-5521, Pages:1008-1017