Robert Dickinson

Summary

Affiliation: Imperial College
Country: UK

Publications

  1. ncbi request reprint Competitive inhibition at the glycine site of the N-methyl-D-aspartate receptor by the anesthetics xenon and isoflurane: evidence from molecular modeling and electrophysiology
    Robert Dickinson
    Blackett Laboratory, Imperial College London, South Kensington, London SW7 2AZ, United Kingdom
    Anesthesiology 107:756-67. 2007
  2. pmc Bench-to-bedside review: Molecular pharmacology and clinical use of inert gases in anesthesia and neuroprotection
    Robert Dickinson
    Biophysics Section, Blackett Laboratory, Imperial College London, South Kensington, London SW7 2AZ, UK
    Crit Care 14:229. 2010
  3. doi request reprint Competitive inhibition at the glycine site of the N-methyl-D-aspartate receptor mediates xenon neuroprotection against hypoxia-ischemia
    Paul 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
  4. doi request reprint 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 binding
    Scott P Armstrong
    Biophysics Section, Imperial College London, London, United Kingdom
    Anesthesiology 117:38-47. 2012
  5. ncbi request reprint Determinants of the anesthetic sensitivity of two-pore domain acid-sensitive potassium channels: molecular cloning of an anesthetic-activated potassium channel from Lymnaea stagnalis
    Isabelle Andres-Enguix
    Biophysics Section, Blackett Laboratory, and Division of Biology, Imperial College, South Kensington, London SW7 2AZ
    J Biol Chem 282:20977-90. 2007

Collaborators

  • Nicholas P Franks
  • Scott P Armstrong
  • Paul Banks
  • Isabelle Andres-Enguix
  • Christopher J Edge
  • Thomas J W McKitrick
  • Catharine H Geldart
  • Rohan Babla
  • Paul J Banks
  • Constantinos Simillis
  • Pietro D Spanu
  • Mervyn Maze
  • Alex Caley
  • Raquel Yustos
  • Mark A Schumacher

Detail Information

Publications5

  1. ncbi request reprint Competitive inhibition at the glycine site of the N-methyl-D-aspartate receptor by the anesthetics xenon and isoflurane: evidence from molecular modeling and electrophysiology
    Robert 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...
  2. pmc Bench-to-bedside review: Molecular pharmacology and clinical use of inert gases in anesthesia and neuroprotection
    Robert 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...
  3. doi request reprint Competitive inhibition at the glycine site of the N-methyl-D-aspartate receptor mediates xenon neuroprotection against hypoxia-ischemia
    Paul 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...
  4. doi request reprint 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 binding
    Scott 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...
  5. ncbi request reprint Determinants of the anesthetic sensitivity of two-pore domain acid-sensitive potassium channels: molecular cloning of an anesthetic-activated potassium channel from Lymnaea stagnalis
    Isabelle 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...