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The William Harvey Research Institute - Faculty of Medicine and Dentistry

Dr Rebecca Charles


BHF Intermediate Research Fellow

Centre: Clinical Pharmacology and Precision Medicine

Telephone: +44(0) 20 7882 6865


Rebecca 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.


Soluble 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.

Key Publications

  • Charles RL, Abis G, Fernandez, BF, Guttzeit S, Conte MR, A thiol redox sensor in soluble epoxide hydrolase enables oxidative activation by intra-protein disulfide bond formation. Redox Biol. 2021, 46:102107.
  • Cho HJ, Kamynina A, Charles RL, Rudyk O, Ng T, Burgoyne JR, Eaton P. Complex interrelationships between nitro-alkene-dependent inhibition of soluble epoxide hydrolase, inflammation and tumor growth. Redox Biol. 2020 Jan; 29:101405.
  • Abis G, Charles RL, Kopec J, Yue WW, Atkinson RA, Bui TTT, Lynham S, Popova S, Sun YB, Fraternali F, Eaton P, Conte MR.– 15-deoxy-Δ12,14-Prostaglandin J2 inhibits human soluble epoxide hydrolase by a dual orthosteric and allosteric mechanism. Commun Biol. 2019 May 17;2:188.
  • Abis GCharles RLEaton PConte MR. Expression, purification, and characterisation of human soluble Epoxide Hydrolase (hsEH) and of its functional C-terminal domain. Protein Expr Purif. 2018 Sep 12;153:105-113.
  • Charles RL, Rudyk O, Prysyazhna O, Kamynina A, Yang J, Morisseau C, Hammock B, Freeman B, Eaton P. Protection from hypertension in mice by the Mediterranean diet is mediated by nitro fatty acid inhibition of soluble epoxide hydrolase. Proc Natl Acad Sci U S A. 2014 Jun 3;111(22):8167-72.
  • Charles RL, Burgoyne JR, Mayr M, Weldon SM, Hubner N, Landar A, Eaton P. Redox regulation of soluble epoxide hydrolase by 15-deoxy-prostaglandin J2 controls coronary hypoxic vasodilation. Circ Res 108, 324-334 (2011).


Internal: Prof Philip Eaton (WHRI), Dr Roberto Buccafusca (School of Physics and Chemical Sciences)

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