Patient with anaesthesiaAnaesthesia makes up the largest hospital speciality and has a huge role to play in nearly every aspect of any hospital from operating theatres to accident and emergency, to the labour ward, and to intensive care. Our research ranges from basic molecular research into mechanisms of anaesthesia to investigating the clinical impact of novel anaesthetic agents. 

Our research covers the entirety of patient’s perioperative journey and through this, we aim to deliver the greatest impact. The section has been pioneering in the development of novel technologies to facilitate the delivery of anaesthetic agents and has also made pivotal in-roads into the mechanism of action of anaesthetic agents and their wider application to other diseases (such as their protective roles in brain injury and in cancer).

Research themes:

Search or filter publications

Filter by type:

Filter by publication type

Filter by year:

to

Results

  • Showing results for:
  • Reset all filters

Search results

  • Journal article
    Tatham K, Donaldson H, O'Dea K, Wakabayashi K, Marczin N, Takata Met al., 2013,

    Marginated monocytes play a central role in lung ischaemia-reperfusion injury in mice: Implications for lung transplantation

    , EUROPEAN RESPIRATORY JOURNAL, Vol: 42, ISSN: 0903-1936
  • Conference paper
    Harris K, Campos-Pires R, Kiru L, Franks NP, Dickinson Ret al., 2013,

    The NMDA receptor glycine site mediates xenon neuroprotection against traumatic brain injury in vitro

    , British Neuroscience Association Meeting
  • Journal article
    Kastsouri L, Vizcaychipi M, McArthur S, Harrison I, Suarez-Calvet M, Lleo A, Lloyd D, Ma D, Sastre Met al., 2013,

    Prazosin, a α1-adrenoceptor antagonist, prevents memory deficits in the APP23 transgenic mouse model of Alzheimer's disease

    , Neurobiology of Aging, Vol: 34, Pages: 1105-1115
  • Conference paper
    Geldart CH, McKitrick TJW, Armstrong SP, Banks SP, Edge CJ, Babla R, Simillis C, Franks NP, Dickinson Ret al., 2012,

    Identification of two mutations (F758W & F758Y) in the N-Methyl-D-Aspartate receptor glycine-binding site that selectively prevent competitive inhibition by xenon without affecting glycine binding

    , Anaesthetic Research Society Meeting, London
  • Conference paper
    Armstrong SP, Banks P, McKitrick T, Geldart C, Edge C, Babla R, Simillis C, Franks NP, Dickinson Ret al., 2012,

    Mutations in the NMDA receptor glycine site prevent competitive inhibition by xenon without affecting inhibition by sevoflurane or isoflurane

    , Society for Neuroscsince Meeting, New Orleans
  • Journal article
    Li Z, Yang Y, Lu Y, Liu D, Xu E, Jia J, Yang D, Zhang X, Yang H, Ma D, Wang Net al., 2012,

    Intraocular pressure <i>vs</i> intracranial pressure in disease conditions: A prospective cohort study (Beijing iCOP study)

    , BMC NEUROLOGY, Vol: 12, ISSN: 1471-2377
  • Journal article
    Armstrong SP, Banks PJ, McKitrick TJW, Geldart CHG, Edge CJE, Babla R, Simillis C, Franks NP, Dickinson Ret al., 2012,

    Identification of two mutations (F758W & F758Y) in the NMDA receptor glycine-binding site that prevent competitive inhibition by xenon without affecting glycine binding

    , Anesthesiology, Vol: 117, Pages: 38-47, ISSN: 1528-1175

    BACKGROUND: Xenon is a general anesthetic with neuroprotective properties. Xenon inhibition at the glycine-binding site of the N-Methyl-D-aspartate (NMDA) receptor mediates xenon neuroprotection against ischemic injury in vitro. 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.METHODS:Site-directed mutagenesis was used to mutate specific amino-acids in the GluN1 subunit of rat NMDA receptors. Mutant GluN1/GluN2A receptors were expressed in HEK 293 cells and were assessed functionally using patch-clamp electrophysiology. The responses of the mutant receptors to glycine and anesthetics were determined.RESULTS:Mutation of phenylalanine 758 to an aromatic tryptophan or tyrosine left glycine affinity unchanged, but eliminated xenon binding without affecting the binding of sevoflurane or isoflurane.CONCLUSIONS:These findings confirm xenon binds to the glycine site of the GluN1 subunit of the NMDA receptor and indicate that interactions between xenon and the aromatic ring of the phenylalanine 758 residue are important for xenon binding. Our most important finding is that we have identified two mutations, F758W and F758Y, that eliminate xenon binding to the NMDA receptor glycine site without changing the glycine affinity of the receptor or the binding of volatile anesthetics. The identification of these selective mutations will allow knock-in animals to be used to dissect the mechanism(s) of xenon's neuroprotective and anesthetic properties in vivo.
  • Journal article
    Vizcaychipi MP, Xu L, Barreto G, Ma D, Maze M, Giffard Ret al.,

    Heat Shock Protein 72 Overexpression Prevents Early Postoperative Cognitive Dysfunction following Orthopedic Surgery under General Anesthesia in Mice

    , Anaesthesiology
  • Journal article
    Zych B, Popov AF, Stavri G, Bashford A, Bahrami T, Amrani M, De Robertis F, Carby M, Marczin N, Simon AR, Redmond KCet al., 2012,

    Early outcomes of bilateral sequential single lung transplantation after ex-vivo lung evaluation and reconditioning

    , JOURNAL OF HEART AND LUNG TRANSPLANTATION, Vol: 31, Pages: 274-281, ISSN: 1053-2498
  • Journal article
    Vizcaychipi MP, Lloyd DG, Wan Y, Palazzo MG, Maze M, Ma Det al., 2011,

    Xenon Pretreatment May Prevent Early Memory Decline after Isoflurane Anesthesia and Surgery in Mice

    , PLOS ONE, Vol: 6, ISSN: 1932-6203

This data is extracted from the Web of Science and reproduced under a licence from Thomson Reuters. You may not copy or re-distribute this data in whole or in part without the written consent of the Science business of Thomson Reuters.

Request URL: http://www.imperial.ac.uk:80/respub/WEB-INF/jsp/search-t4-html.jsp Request URI: /respub/WEB-INF/jsp/search-t4-html.jsp Query String: id=910&limit=10&page=4&respub-action=search.html Current Millis: 1732438984144 Current Time: Sun Nov 24 09:03:04 GMT 2024