Affiliation: Imperial College
- Competitive inhibition at the glycine site of the N-methyl-D-aspartate receptor by the anesthetics xenon and isoflurane: evidence from molecular modeling and electrophysiologyRobert Dickinson
Blackett Laboratory, Imperial College London, South Kensington, London SW7 2AZ, United Kingdom
Anesthesiology 107:756-67. 2007..However, the site of action of these agents on the NMDA receptor is unknown. The authors show that xenon and isoflurane compete for the binding of the coagonist glycine on the NMDA receptor NR1 subunit...
- Bench-to-bedside review: Molecular pharmacology and clinical use of inert gases in anesthesia and neuroprotectionRobert Dickinson
Biophysics Section, Blackett Laboratory, Imperial College London, South Kensington, London SW7 2AZ, UK
Crit Care 14:229. 2010..We summarize recent in vitro and in vivo studies on the actions of helium and the other inert gases, and discuss their potential to be used as neuroprotective agents...
- Competitive inhibition at the glycine site of the N-methyl-D-aspartate receptor mediates xenon neuroprotection against hypoxia-ischemiaPaul Banks
Biophysics Section, Blackett Laboratory, Department of Anaesthetics, Pain Medicine and Intensive Care, Imperial College London, London SW7 2AZ, United Kingdom
Anesthesiology 112:614-22. 2010..Xenon inhibits NMDA receptors by competing with glycine at the glycine-binding site. We test the hypothesis that inhibition of the NMDA receptor at the glycine site underlies xenon neuroprotection against hypoxia-ischemia...
- Identification of two mutations (F758W and F758Y) in the N-methyl-D-aspartate receptor glycine-binding site that selectively prevent competitive inhibition by xenon without affecting glycine bindingScott P Armstrong
Biophysics Section, Imperial College London, London, United Kingdom
Anesthesiology 117:38-47. 2012..Here we identify specific amino acids important for xenon binding to the NMDA receptor, with the aim of finding silent mutations that eliminate xenon binding but leave normal receptor function intact...
- Determinants of the anesthetic sensitivity of two-pore domain acid-sensitive potassium channels: molecular cloning of an anesthetic-activated potassium channel from Lymnaea stagnalisIsabelle Andres-Enguix
Biophysics Section, Blackett Laboratory, and Division of Biology, Imperial College, South Kensington, London SW7 2AZ
J Biol Chem 282:20977-90. 2007..The L159A mutation in LyTASK disrupts the stereoselective response to isoflurane while having no effect on the pH sensitivity of the channel, suggesting this critical amino acid may form part of an anesthetic binding site...