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Molecular Pharmacology of N-Methyl-D-aspartate glutamate receptors

  • Full or part time
  • Application Deadline
    Applications accepted all year round
  • Self-Funded PhD Students Only
    Self-Funded PhD Students Only

Project Description

Fast neuronal communication at synaptic contacts relies on neurotransmitter release from the presynaptic terminal and the majority of excitatory neurotransmission within the mammalian central nervous system is mediated by the neurotransmitter glutamate. Glutamate acts on a number of ligand gated ion channels often referred to as ’ionotropic’ receptors which when opened permit ion flux across the cell membrane and result in a change in neuronal excitability. One subtype of ionotropic glutamate receptor is the N-methyl-D-aspartate receptor (NMDAR) and these receptors play a number of roles in normal and abnormal processes within the central nervous system (CNS), ranging from learning and memory to excitotoxic neuronal cell death following stroke or brain trauma. The involvement of NMDARs in such a broad range of CNS processes and disorders has triggered a great deal of interest in understanding the molecular determinants of NMDAR function. This knowledge is not only required for teasing apart the complex mechanisms of receptor action but may also assist in the development of therapeutic strategies to combat the neurological damage induced by NMDAR overactivity.

NMDARs are heteromeric protein complexes made up of different types of subunit and my laboratory is interested in understanding how specific regions or ’functional’ domains within these receptor subunits can specify distinct pharmacological or functional properties. We are also interested in exploring the impact of NMDARs with altered pharmacological properties on neuronal function. The laboratory is a using variety of molecular biological, biochemical and functional methods to understand the roles played by these domains in receptor function and pharmacology.


Recent publications:

1. Chen P E, Geballe M T, Katz E, Erreger K, Livesey M R, O'Toole K K, Le P, Lee C J, Snyder J P, Traynelis S F and Wyllie D J. Modulation of glycine potency in rat recombinant NMDA receptors containing chimeric NR2A/2D subunits expressed in Xenopus laevis oocytes. (2008) Journal of Physiology. 586:227-45.

2. Wrighton D C, Baker E J, Chen P E and Wyllie D J. Mg2+ and memantine block of rat recombinant NMDA receptors containing chimeric NR2A/2D subunits expressed in Xenopus laevis oocytes. (2008) Journal of Physiology. 586:211-25.

3. Erreger K, Geballe M T, Kristensen A, Chen P E, Hansen K B, Lee C J, Yuan H, Le P, Lyuboslavsky P N, Micale N, Jorgensen L, Clausen R P, Wyllie D J, Snyder J P and Traynelis S F. Subunit-specific agonist activity at NR2A-, NR2B-, NR2C-, and NR2D-containing N-methyl-D-aspartate glutamate receptors. (2007) Molecular Pharmacology. 72:907-20.

4. Wyllie DJA and Chen PE. Taking the time to study competitive antagonism. (2007) British Journal of Pharmacology.150: 541-51.

5. Frizelle PA, Chen PE and Wyllie DJA. Equilibrium constants for NVP-AAM077 acting on recombinant NR1/NR2A and NR1/NR2B NMDA receptors: implications for studies of synaptic transmission. (2006) Molecular Pharmacology. 70: 1022-1032.

6. Chen PE and Wyllie DJ. Pharmacological insights obtained from structure-function studies of ionotropic glutamate receptors. (2006) British Journal of Pharmacology. 147:839-53.

7. Chen PE, Geballe MT, Stansfeld PJ, Johnston AR, Yuan H, Jacob AL, Snyder JP, Traynelis SF and Wyllie DJ. Structural features of the glutamate binding site in recombinant NR1/NR2A N-methyl-D-aspartate receptors determined by site-directed mutagenesis and molecular modeling.(2005) Molecular Pharmacology. 67:1470-84.

How good is research at Royal Holloway, University of London in Biological Sciences?

FTE Category A staff submitted: 24.00

Research output data provided by the Research Excellence Framework (REF)

Click here to see the results for all UK universities

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