Richard Evans

Personal Details

Professor of Molecular Physiology and Pharmacology

Department: Molecular and Cell Biology
Telephone:  0116 229 7057
Address: University Rd, LE1 7HB
Web Links:


  • 1990: DPhil, Pharmacology, University of Oxford
  • 1991-1993: Post-doctoral fellow, Vollum Institute, OHSU, Portland, OR, USA
  • 1994-1996: Post doctoral scientist Glaxo Institute for Molecular Biology, Geneva, Switzerland
  • 1996-2001: Lecturer, University of Leicester
  • 2001-2004: Reader, University of Leicester
  • 2004-present: Professor of Molecular Physiology and Pharmacology, University of Leicester


  • Principles of Pharmacology
  • Cardiovascular Physiology & Pharmacology
  • P2X receptors
  • Ion channels


  1. Allsopp, R.C., Dayl, S., Schmid, R & Evans, R.J. (2017). Unique residues in the ATP gated human P2X7 receptor define a novel allosteric pocket for the selective antagonist AZ10606120. Scientific Reports, 7:725.
  2. Fryatt, A.G., Dayl, S., Cullis, P.M., Schmid, R. and Evans, R.J. (2016). Mechanistic insights from resolving ligand-dependent kinetics of conformational changes at ATP-gated P2X1R ion channels. Scientific Reports, 6:32918.
  3. Maître, B, Magnenat, S., Heim, V., Ravanat, C., Evans, R.J., de la Salle, H., Gachet, C. and Hechler, B. (2015). The P2X1 receptor is required for neutrophil extravasation during LPS-induced lethal endotoxemia in mice. J. Immunol. 194:739-749.
  4. Farmer, L.K., Schmid, R and Evans, R.J. (2015). Use of chimeras, point mutants and molecular modelling to map the antagonist binding site of NF449 at P2X1 receptors for ATP. J. Biol. Chem. 290:1599-1569.
  5. White, C.W., Short, J.L., Evans, R.J. and Ventura, S. (2015). Development of a P2X1- purinoceptor mediated contractile response in the aged mouse prostate gland through slowing down of ATP breakdown. Neurology & Urodynamics 34:292-298.
  6. Allsopp, R.C. and Evans, R.J. (2015). Contribution of the juxta-tansmembrane intracellular regions to the time-course and permeation of ATP-gated P2X7 receptor ion channels. J. Biol. Chem. 290:14556-14566.
  7. Jones, S., Evans, R.J. and Mahaut-Smith, M.P. (2014). Calcium Influx through P2X1 Receptors Amplifies P2Y1 Receptor-evoked Calcium Signalling and ADP-evoked Platelet Aggregation. Mol. Pharmacol. 86:243-251.
  8. Darbousset, R., Delierneux, C., Mezouar, S., Hego, A., Lecut, C., Guillaumat, I., Riederer, M.A., Evans, R.J., Dignat-George, F., Panicot-Dubois, L., Oury, C., Dubois, C. (2014). P2X1 expressed on polymorphonuclear neutrophils is required for thrombosis in mice. Blood, 124: 2575-2585.
  9. Fryatt, A.G. and Evans, R.J. (2014). Kinetics of conformational changes revealed by voltage-clamp fluorometry give insight to desensitization at ATP-gated human P2X1 receptors. Mol. Pharmacol. 86:707-715.
  10. Allsopp, R.C., Farmer, L.K., Fryatt, A.G. and Evans, R.J. (2013). P2X receptor chimeras highlight roles of the amino terminus to partial agonist efficacy, the carboxyl terminus to recovery from desensitization, and independent regulation of channel transitions. J. Biol. Chem. 288, 21412-21421.
  11. El-Ajouz, S., Ray, D., Allsopp, R.C. & Evans, R.J. (2012). Molecular basis of selective antagonism of the P2X1 receptor for ATP by NF449 and suramin: contribution of basic amino acids in the cysteine-rich loop. Br. J. Pharmacol., 165, 390-400.
  12. Roberts, J. A., Allsopp, R. C., El Ajouz, S., Vial, C., Schmid, R., Young, M. T. and Evans, R. J. (2012) Agonist binding evokes extensive conformational changes in the extracellular domain of the ATP-gated human P2X1 receptor ion channel. Proc Natl Acad Sci U S A, 109, 4663-4667.
  13. Lecut, C., Faccinetto, C., Delierneux, C., van Oerle, R., Spronk, H. M., Evans, R. J., El Benna, J., Bours, V. and Oury, C. (2012) ATP-gated P2X(1) ion channels protect from endotoxemia by dampening neutrophil activation. J Thromb Haemost, 10, 453-465.
  14. Lalo, U., Jones, S., Mahaut-Smith, M.P. and Evans, R.J. (2012) Heat Shock Protein 90 inhibitors reduce trafficking of ATP-gated P2X1 receptors and human platelet responsiveness. J. Biol. Chem 287, 32747-32754.
  15. Roberts, J.A., Bottrill, A., Mistry, S. and Evans, R.J. (2012) Mass spectrometry analysis of human P2X1 receptors; insight into phosphorylation, modelling and conformational changes. J. Neurochem. 123, 725-735.
  16. Wen, H. & Evans, R.J. (2011). Contribution of the intracellular C terminal domain to regulation of human P2X1 receptors for ATP by phorbol ester and Gq coupled mGlu1a receptors. Eur. J. Pharmacol. 654, 155-159.
  17. Allsopp, R.C., El Ajouz, S., Schmid, R. & Evans, R.J. (2011). Cysteine scanning mutagenesis (residues Glu52-Gly96) of the human P2X1 receptor for ATP; mapping agonist binding and channel gating. J. Biol. Chem., 286, 29207- 29217.
  18. Jones, S., Evans, R.J. & Mahaut Smith M.P. (2011). Extracellular calcium modulates ADP-evoked aggregation through altered agonist degradation:implications for conditions used to study P2Y receptor activation. Br. J. Heamatol. 153, 83-91.
  19. Lalo, U., Roberts, J.A. & Evans, R.J. (2011). Identification of human P2X1 receptor- interacting proteins reveals a role of the cytoskeleton in receptor regulation. J. Biol. Chem., 286, 30591-30599.
  20. Allsopp, R. C. and Evans, R. J. (2011) The intracellular amino terminus plays a dominant role in desensitisation of ATP gated P2X receptor ion channels. J Biol Chem, 286, 44691-44701.
  21. Lalo, U., Allsopp, R.C., Mahaut-Smith, M.P. & Evans, R.J. (2010). P2X1 receptor mobility and trafficking; regulation by receptor insertion and activation. J.Neurochem, 113, 1177-1187.
  22. Allsopp, R.C., Lalo, U. & Evans, R.J. (2010). Lipid raft association and cholesterol sensitivity of P2X1-4 receptors for ATP; chimeras and point mutants identify intracellular amino terminal residues involved in lipid regulation of P2X1 receptors. J. Biol. Chem. 285, 32770-32777.


Molecular basis of properties of P2X receptors for ATP

P2X receptors for ATP are ligand gated cation channels that comprise a distinct family of ligand gated cation channels with two transmembrane domains, intracellular amino and carboxy termini and a large extracellular ligand binding loop. Seven P2X receptor genes have been cloned (P2X1-7) and they form functional homo-and heteromeric channels with a range of phenotypes.

A major focus of our work has been to understand the molecular basis of drug action at P2X receptors. We have used a site directed mutagenesis approach coupled with molecular modelling (with Ralf Schmid) to develop a models of ligand action (agonists and antagonists). The crystalization of a range of P2X receptors has been a major advance for our understanding of the molecular basis of their properties. These provide snapshots of some receptor conformations and experimental evidence suggests that existence of additional states. Work in the lab is focused on understand the transitions between different states of the receptor and providing validated models for “missing conformations” of the receptor.

Current project in the laboratory include:

  1. Using cross-linking and bioinformatics approaches to model the intracellular regions of the P2X receptor.
  2. Mapping the extent of conformational flexibility in different states of the P2X receptor.
  3. Understanding the basis of antagonist action at P2X7 receptors.


Understanding the molecular basis of P2X receptor properties and how this can be used to aid in drug development.

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