Wellcome Trust Multi User Equipment Award for 'Using Structural Mass Spectrometry for the Study of Large Macromolecular Machines'
Published: Nov 10, 2014 10:50:48 AM
Published: Nov 10, 2014 10:45:47 AM
Published: Nov 10, 2014 10:41:30 AM
Andrea Townsend Nicholson
Dr Andrea Townsend-Nicholson Senior Lecturer
Tel: 020 7679 2237
Room 105, Darwin Building
I am interested in understanding how extracellular signals are transduced into intracellular responses. I aim to enhance our current understanding of the molecular basis of health and disease and my research focuses primarily on elucidating the role of cell surface receptors in these processes. My work involves the use of molecular biology, biochemistry, cell biology, cellular imaging, cell signalling and molecular pharmacology to study purinergic, glutamatergic, GABAergic and dopaminergic responses in the cardiovascular system and in the central nervous system.
My teaching interests extend to the development and use of novel technology and assessment methodologies to enhance student learning (www.brightida.com). I presently teach Molecular Biology to first year Medical students (Phase I) and first year undergraduates taking BIOC1001/1008/1009, to second year students taking molecular biology (BIOC2001) and I lecture in cell signalling and molecular biology on several third year courses (BIOC3004, BIOC3005), including the third year research project (BIOC3002/3009)
I obtained my Bachelor of Science degree in Molecular Genetics and
Molecular Biology, with a Major in Zoology and (somehow) a Minor in
Religion, from the University of Toronto in 1986. I subsequently studied
at the Laboratoire de Génétique Moléculaire des Eucaryotes (LGME) in
Strasbourg France, investigating the establishment of the dorsoventral
polarity axis in Drosophila melanogaster. I obtained my doctorate in
Cellular and Molecular Biology from the Université Louis Pasteur in
1990. From 1991 to 1996, I moved from transcriptional studies to cell
signalling, studying mammalian G protein-coupled receptors as a
postdoctoral fellow in the Neurobiology Division of the Garvan Institute
of Medical Research (Sydney, Australia). During this time, I cloned and
characterised several adenosine receptor subtypes and learned about the
benefits of wide-brimmed hats and factor 50 sunscreen. Having started
my research career at University College (University of Toronto) in
Canada, I am now at University College London, where I was appointed as a
member of academic staff in the Department of Biochemistry &
Molecular Biology in 2001, following three and a half years of
postdoctoral study in the Department of Anatomy & Developmental
Biology and eighteen months as a British Heart Foundation Intermediate
Research Fellow in the Department of Physiology.
Molecular Mechanisms of Purinoceptor Function
The extracellular signalling molecules ATP and UTP modulate purinergic, and pyrimidinergic, transmission in the central, peripheral and enteric nervous systems by activating specific ionotropic (P2X) or metabotropic (P2Y) cell-surface receptors (purinoceptors). ATP is hydrolysed to adenosine, itself a neuromodulator, which acts through metabotropic adenosine receptor subtypes (P1 purinoceptors). Despite the ubiquity of both purinergic ligands and purinoceptors, the differential expression of the large number of purinoceptor subtypes and the different components of their downstream signal transduction pathways allows for the generation of very specific physiological responses in a particular cell type or tissue. The research in the lab is directed towards enhancing our current understanding of the molecular basis of health and disease, using purinoceptors as a model system. Research projects are aimed at investigating the structural and functional diversity of purinoceptors, the molecular mechanisms underlying purinoceptor signal transduction and the role of purinoceptors in disease states.
Schematic diagram of the human A1 adenosine receptor, indicating (in red) the residues that have been mutated for ligand binding studies. The transmembrane domains are located within the boxed structure, which represents the plasma membrane. The NH2-terminus is located extracellularly and the COOH-terminus is intracellular.
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