Dr Rebecca CharlesBHF Intermediate Research FellowCentre: Clinical Pharmacology and Precision MedicineEmail: r.charles@qmul.ac.ukTelephone: +44(0) 20 7882 6865ProfileResearchPublicationsSponsorsCollaboratorsNewsProfileRebecca gained a BSc in Biochemistry from The University of Birmingham in 2002 before working at Unilever for 3 years, where she was involved in a variety of different skin ageing and skin health projects including a number of clinical trials. Rebecca then undertook her PhD studies within the School of Cardiovascular Medicine & Sciences at King’s College London. In 2017, Rebecca received a BHF Intermediate Fellowship to investigate activation of soluble Epoxide Hydrolase by intra-protein disulfide formation. In 2019, she moved to the William Harvey Research Institute, Queen Mary University of London where her group studies the molecular basis of redox sensing and signalling in soluble epoxide hydrolase and its importance to the cardiovascular and pulmonary systems.ResearchSoluble epoxide hydrolase (sEH) is ubiquitously expressed, including in cardiovascular-relevant tissues such as endothelial or vascular smooth muscle cells as well as cardiomyocytes, where it is an important modulator of arterial and cardiac functions. sEH is also a susceptibility factor for human heart failure, with polymorphisms that enhance hydrolase activity increasing cardiovascular risk. Conversely, inhibitors (or transgenic knock-outs) of sEH offer a broad spectrum of cardiovascular protection, including blockade of smooth muscle proliferation, reduction of atherosclerosis and hypertension, prevention and regression of cardiac hypertrophy and HF, and fibrosis. Until 2009, little was known about how sEH activity was regulated and it was thought to be principally determined by its expression abundance. However, it is now apparent that a number of different oxidative post-translational modifications regulate this hydrolase. My research focuses on defining and understanding the molecular basis of redox sensing and signalling in sEH and its importance to the cardiovascular and pulmonary systems.Publications de Jesus DS, Buffonge S, Abis G et al. (2024). Zinc-mediated inhibition of soluble epoxide hydrolase promotes pulmonary hypertension. nameOfConference DOI: 10.1016/j.freeradbiomed.2024.10.125 QMRO: https://qmro.qmul.ac.uk/xmlui/handle/123456789/103127 Faulkes CG, Eykyn TR, Miljkovic JL et al. (publicationYear). Naked mole-rats have distinctive cardiometabolic and genetic adaptations to their underground low-oxygen lifestyles. nameOfConference DOI: 10.1038/s41467-024-46470-x QMRO: https://qmro.qmul.ac.uk/xmlui/handle/123456789/96659 Caggiano MF, Charles R, Prysyazhna O et al. (2023). UK-5099 does not inhibit the mitochondrial pyruvate carrier through irreversible adduction to cysteine 54 in MPC2. nameOfConference DOI: 10.1016/j.freeradbiomed.2023.10.148 QMRO: https://qmro.qmul.ac.uk/xmlui/handle/123456789/92439 Charles R, Fernandez-Caggiano M, Rudyk O et al. (2022). A novel inhibitor of soluble Epoxide Hydrolase that adducts C521 is cardioprotective. nameOfConference DOI: 10.1016/j.freeradbiomed.2022.10.090 QMRO: https://qmro.qmul.ac.uk/xmlui/handle/123456789/92464 Charles R, Eaton P (publicationYear). Redox Regulation of Soluble Epoxide Hydrolase—Implications for Cardiovascular Health and Disease. nameOfConference DOI: 10.3390/cells11121932 QMRO: https://uat2-qmro.qmul.ac.uk/xmlui/handle/123456789/79463 Charles RL, Abis G, Fernandez BF et al. (2021). A thiol redox sensor in soluble epoxide hydrolase enables oxidative activation by intra-protein disulfide bond formation. nameOfConference DOI: 10.1016/j.redox.2021.102107 QMRO: https://uat2-qmro.qmul.ac.uk/xmlui/handle/123456789/73901 Cho H-J, Switzer CH, Kamynina A et al. (2020). Complex interrelationships between nitro-alkene-dependent inhibition of soluble epoxide hydrolase, inflammation and tumor growth. nameOfConference DOI: 10.1016/j.redox.2019.101405 QMRO: https://uat2-qmro.qmul.ac.uk/xmlui/handle/123456789/73986 Abis G, Charles RL, Kopec J et al. (publicationYear). 15-deoxy-Δ12,14-Prostaglandin J2 inhibits human soluble epoxide hydrolase by a dual orthosteric and allosteric mechanism. nameOfConference DOI: 10.1038/s42003-019-0426-2 QMRO: https://uat2-qmro.qmul.ac.uk/xmlui/handle/123456789/73990 Dunham-Snary KJ, Wu D, Potus F et al. (2019). Ndufs2, a Core Subunit of Mitochondrial Complex I, Is Essential for Acute Oxygen-Sensing and Hypoxic Pulmonary Vasoconstriction. nameOfConference DOI: 10.1161/circresaha.118.314284 QMRO: https://uat2-qmro.qmul.ac.uk/xmlui/handle/123456789/73987 Abis G, Charles RL, Eaton P et al. (2019). Expression, purification, and characterisation of human soluble Epoxide Hydrolase (hsEH) and of its functional C-terminal domain. nameOfConference DOI: 10.1016/j.pep.2018.09.001 QMRO: https://uat2-qmro.qmul.ac.uk/xmlui/handle/123456789/73988 Bassi R, Burgoyne JR, DeNicola GF et al. (2017). Redox-dependent dimerization of p38α mitogen-activated protein kinase with mitogen-activated protein kinase kinase 3. nameOfConference DOI: 10.1074/jbc.m117.785410 QMRO: https://uat2-qmro.qmul.ac.uk/xmlui/handle/123456789/73927 Charles RL, Rudyk O, Prysyazhna O et al. (2014). Protection from hypertension in mice by the Mediterranean diet is mediated by nitro fatty acid inhibition of soluble epoxide hydrolase. nameOfConference DOI: 10.1073/pnas.1402965111 QMRO: qmroHref Charles RL, Rudyk O, Prysyazhna O et al. (2013). PSS135 Loss of Redox Regulation in Cys521Ser Soluble Epoxide Hydrolase Knock-In Mice Results in Hypertension and Hypertrophy. nameOfConference DOI: 10.1016/j.freeradbiomed.2013.10.554 QMRO: qmroHref Charles R, Jayawardhana T, Eaton P (2014). Gel-based methods in redox proteomics. nameOfConference DOI: 10.1016/j.bbagen.2013.04.021 QMRO: qmroHref Charles R, Yin X, Mayr M et al. (2012). Detection and Identification of Cardiac Proteins Modified by the Dietary Flavanol Curcumin. nameOfConference DOI: 10.1016/j.freeradbiomed.2012.10.430 QMRO: qmroHref Schroder E, Prysyazhna O, Charles R et al. (2012). Detection of Systemic Modification of Proteins in Mice by Sulforaphane after Oral Consumption. nameOfConference DOI: 10.1016/j.freeradbiomed.2012.10.479 QMRO: qmroHref Ray R, Murdoch CE, Wang M et al. (2011). Endothelial Nox4 NADPH Oxidase Enhances Vasodilatation and Reduces Blood Pressure In Vivo. nameOfConference DOI: 10.1161/atvbaha.110.219238 QMRO: qmroHref Charles RL, Burgoyne JR, Mayr M et al. (2011). Redox Regulation of Soluble Epoxide Hydrolase by 15-Deoxy-&Dgr;-Prostaglandin J2 Controls Coronary Hypoxic Vasodilation. nameOfConference DOI: 10.1161/circresaha.110.235879 QMRO: qmroHref Madhani M, Hall AR, Cuello F et al. (2010). Phospholemman Ser69 phosphorylation contributes to sildenafil-induced cardioprotection against reperfusion injury. nameOfConference DOI: 10.1152/ajpheart.00129.2010 QMRO: qmroHref Charles RL, Burgoyne J, Mayr M et al. (2009). 15-deoxy-Δ 12, 14-prostaglandin J2 Adducts to Soluble Epoxide Hydrolase at Cys521 Resulting in its Inhibition which Couples to Coronary Vasodilation. nameOfConference DOI: doi QMRO: qmroHref Charles RL, Eaton P (2008). Redox signalling in cardiovascular disease. nameOfConference DOI: 10.1002/prca.200780104 QMRO: qmroHref Burgoyne JR, Madhani M, Cuello F et al. (2007). Cysteine Redox Sensor in PKGIa Enables Oxidant-Induced Activation. nameOfConference DOI: 10.1126/science.1144318 QMRO: qmroHref Charles RL, Schröder E, May G et al. (2007). Protein Sulfenation as a Redox Sensor Proteomics Studies Using a Novel Biotinylated Dimedone Analogue*. nameOfConference DOI: 10.1074/mcp.m700065-mcp200 QMRO: qmroHref Burgoyne JR, Madhani M, Cuello F et al. (2007). H2O2 operates as an endothelium-derived hyperpolarizing factor by directly activating protein kinase G (PKG) Iα independently of cGMP via disulfide formation. nameOfConference DOI: doi QMRO: qmroHref Sponsors British Heart Foundation CollaboratorsInternal Prof Philip Eaton (WHRI) Dr Roberto Buccafusca (School of Physics and Chemical Sciences) News Olive oil and salad combined 'explain' Med diet success (BBC News), May 2014 Olive oil on salad may save your life (The Telegraph), May 2014 Back to top