School of Life and Health Sciences Aston University Aston Triangle Birmingham B4 7ET UK
Email: firstname.lastname@example.org Telephone: +44 (0) 121 204 3997
Fax: +44 (0) 121359 5142
Molecular Biomedical Research
Aston Research Centre for Healthy Ageing (ARCHA)
I graduated in Natural Sciences from Cambridge University in 1981 and then stayed to do a Ph.D in the pharmacology department under the supervision of Prof. Sir Arnold Burgen. I subsequently did post-doctoral work at the National Institute for Medical Research, working with Drs Ed Hulme and Nigel Birdsall and then at the MRC Molecular Neurobiology Unit in Cambridge with Dr Mike Hanley. It was here that I first started to work on the pharmacology of calcitonin gene related peptide (CGRP). I was appointed to a lectureship at Aston University in 1991 where I have continued my work on this and allied peptides.
PH1401: Physiology. PH2501 (module coordinator): Pharmacology
1982 - 1985 PhD University of Cambridge
1978 - 1982 BA, Pharmacology (Class I), University of Cambridge
I specialise in the teaching of molecular pharmacology, especially cell receptors and signal transduction. I also teach general pharamacology and physiology, cell biology and biochemistry. I teach at all levels of the programme from 1st year to M.Sc. and I am head of the pharmacology teaching group. Main modules taught:
Both CGRP and adrenomedullin produce their effects at G-protein coupled receptors (GPCRs). Something like 70% of all drugs act at GPCRs; thus this family is of particular interest in drug discovery. However, the receptors for CGRP and adrenomedullin are of especial interest as they are made up of two subunits; a most unusual arrangement for GPCRs. They share a common subunit called calcitonin receptor-like receptor (CRLR or CL). This has the structure of a typical GPCR with seven transmembrane helices. However, to respond to CGRP a second protein is required, called receptor activity modifying protein 1 (RAMP1). When CL complexes with the related proteins RAMP2 or RAMP3, adrenomedullin receptors are formed.
Higher Education Academy, Biochemical Society, British Pharmacological Society.
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