Zobrazeno 1 - 7
of 7
pro vyhledávání: '"George B. Dawe"'
Autor:
Mohammad Fahim Kadir, Camilo Navarrete, Christian Fuentes, R. Venskutonyte, M. Arsenault, Amanda M Perozzo, E.A. Santander, Y. Yan, John Michael Edwardson, Ryan P.D. Alexander, Derek Bowie, Jette S. Kastrup, Mark R. P. Aurousseau, Karla Frydenvang, Nelson P. Barrera, George B. Dawe
Publikováno v:
Neuron. 102(5)
Summary Neurotransmitter-gated ion channels are allosteric proteins that switch on and off in response to agonist binding. Most studies have focused on the agonist-bound, activated channel while assigning a lesser role to the apo or resting state. He
Autor:
Maria Musgaard, Derek Bowie, Mark R. P. Aurousseau, Elizabeth D. Andrews, Bryan A. Daniels, George B. Dawe, Philip C. Biggin
Glutamate is the major excitatory neurotransmitter in the brain, activating ionotropic receptors named for their selectivity to the agonists NMDA, AMPA, and kainate (KARs). The KAR subunit GluK2 requires external ions, in addition to glutamate, to pr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b31fc6f9bf95a5f690af8eccab126748
https://ora.ox.ac.uk/objects/uuid:cbb20fad-d794-41b8-968d-0be17447fb9c
https://ora.ox.ac.uk/objects/uuid:cbb20fad-d794-41b8-968d-0be17447fb9c
Autor:
George B. Dawe, Derek Bowie
Publikováno v:
Biophysical Journal. 110(3)
Ionotropic glutamate receptors (iGluRs) are ligand-gated ion channels that mediate excitation in the mammalian central nervous system. Amongst iGluRs, the AMPA receptor (AMPAR) subfamily facilitates the initial depolarization of postsynaptic terminal
Publikováno v:
Biophysical Journal. 108(2)
Ionotropic glutamate receptors (iGluRs) facilitate the bulk of synaptic excitation in the mammalian central nervous system. Structures of full-length, AMPA-type iGluRs (AMPARs) have recently been reported in conformations thought to represent resting
Autor:
Philip C. Biggin, Maria Musgaard, George B. Dawe, Bryan A. Daniels, Derek Bowie, Mark R. P. Aurousseau
Publikováno v:
Biophysical Journal. 106(2)
The cation-binding pocket is integral to the stability of the kainate receptor dimer interface, allowing proper activation of the receptor. Interestingly, a double cysteine mutation (Y521C/L783C GluK2) across the interface eliminates the need for occ
Autor:
George B. Dawe, Maria Musgaard, Philip C. Biggin, Derek Bowie, Mark R. P. Aurousseau, Bryan A. Daniels
Publikováno v:
Biophysical Journal. 108(2):287a-288a
Ionotropic glutamate receptors (iGluRs) are vital for the function of our central nervous system (CNS), e.g. in learning and memory formation, and thus implicated in many CNS disorders. The tetrameric iGluRs contain a glutamate-gated cation channel w
Publikováno v:
Parasitology international. 62(6)
We have isolated two genes, Hco-lgc-53 and Hco-mod-1, from the parasitic nematode Haemonchus contortus, which are orthologs of previously characterized genes that encode dopamine and serotonin-gated chloride channels, respectively, in Caenorhabditis