Christopher A. Reynolds
Professor
School of Biological Sciences
University of Essex
United Kingdom
Biography
2000 - present Professor, Department of Biological Sciences, University of Essex 1998-2000 Reader, Department of Biological Sciences, University of Essex 1991-1997 Lecturer, Department of Chemistry and Biological Chemistry, University of Essex 1985-1991 PDRA, Laboratory of Physical Chemistry and Oxford Centre for Molecular Sciences, University of Oxford - under Prof. W. Graham Richards 1982-1985 PhD in Computational Chemistry, University of St. Andrews - under Dr. Colin Thomson 1979-1982 Research Chemist, British Steel 1975-1979 1st class BSc (Honours) Chemistry, University of St. Andrews Professional qualifications: CChem, FRSC Professional activities MRC Research Leader Fellow (2011-2014) Fellow of the Royal Society of Chemistry (RSC), RSC Departmental Representative RSC Theoretical Chemistry Group (Committee member (2012-2014) Biochemical Society, member British Association for Cancer Research (BACR), member
Research Interest
Molecular Modelling Computational Chemistry The development of methods in computational chemistry and bioinformatics and their application to problems in chemistry and biology. Modelling polarization through induced charges Fragment-based drug design Modelling G-protein coupled receptor structure and activation (Class A and Class B) Developing software for molecular modelling (see group web pages)
Publications
-
Wootten, D., Reynolds, C. A., Koole, C., Smith, K. J., Mobarec, J. C., Simms, J., Quon, T., Coudrat, T., Furness, S. G., and Miller, L. J. (2016) A hydrogen-bonded polar network in the core of the glucagon-like peptide-1 receptor is a fulcrum for biased agonism: lessons from class B crystal structures. Mol. Pharmacol. 89,335-347.
-
Wootten, D., Reynolds, C. A., Smith, K. J., Mobarec, J. C., Furness, S. G., Miller, L. J., Christopoulos, A., and Sexton, P. M. (2016) Key interactions by conserved polar amino acids located at the transmembrane helical boundaries in Class B GPCRs modulate activation, effector specificity and biased signalling in the glucagon-like peptide-1 receptor. Biochem. Pharmacol. 118,68-87.
-
Wootten, D., Reynolds, C. A., Smith, K. J., Mobarec, J. C., Koole, C., Savage, E. E., Pabreja, K., Simms, J., Sridhar, R., and Furness, S. G. (2016) The extracellular surface of the GLP-1 receptor is a molecular trigger for biased agonism. Cell 165,1632-1643. doi.org/10.1016/j.cell.2016.05.023
