Zobrazeno 1 - 10
of 13
pro vyhledávání: '"Helen J. Meadows"'
Autor:
Tim Dale, Helen J. Meadows, Andrew J. Powell, Jeffrey J. Clare, Emma C. Hollands, Andrew Baxter, Derek J. Trezise
Publikováno v:
SLAS Discovery. 14:769-780
Gamma-amino butyric acid (GABA)-activated Cl- channels are critical mediators of inhibitory postsynaptic potentials in the CNS. To date, rational design efforts to identify potent and selective GABA(A) subtype ligands have been hampered by the absenc
Publikováno v:
Molecular and Cellular Neuroscience. 37:32-39
Two-pore domain potassium (K(2P)) channels are proposed to underlie the background or leak current found in many excitable cells. Extensive studies have been performed investigating the inhibition of K(2P)2.1 by Galpha(q)- and Galpha(s)-coupled G-pro
Autor:
Emma C. Hollands, Derek J. Trezise, Victoria H John, David L. Downie, Mao Xiang Chen, Tim Dale, Leanne Partington, Helen J. Meadows
Publikováno v:
SLAS Discovery. 12:50-60
Planar array electrophysiology techniques were applied to assays for modulators of recombinant hIK and hSK3 Ca2+-activated K+ channels. In CHO-hIK-expressing cells, under asymmetric K+ gradients, small-molecule channel activators evoked time- and vol
Publikováno v:
The Journal of Physiology. 560:51-62
Background potassium channels control the resting membrane potential of neurones and regulate their excitability. Two-pore-domain potassium (2-PK) channels have been shown to underlie a number of such neuronal background currents. Currents through hu
Autor:
J.E Cluderay, C.W Gray, Paula J. Green, G.J Hervieu, Helen J. Meadows, Jennie L Ranson, Andrew D. Randall
Publikováno v:
Neuroscience. 103:899-919
TREK-1 is a member of the two-pore-domain potassium channel family which is expressed predominantly in the CNS. Using an anti-peptide polyclonal antiserum, we have determined the distribution of TREK-1 in the brain and spinal cord of adult rats. Spec
Autor:
Helen J. Meadows, Andrew D. Randall
Publikováno v:
Neuropharmacology. 40:551-559
Human TASK-3 (hTASK-3) is a recently identified member of the two-pore domain potassium channel (2PDKC) family which in man is predominantly expressed in the cerebellum. Previous preliminary examination of this channel indicates that when expressed i
Autor:
Paul R. Murdock, Graham D Smith, Isro S Gloger, John Terrett, Kathryn Ellington, D.Malcolm Duckworth, Andrew D. Medhurst, Amanda J. L. Barton, Mark H Harries, Christopher D. Benham, Martin J. Gunthorpe, Andrew D. Randall, Helen J. Meadows, Simon Topp, David C. Harrison, Rab K. Prinjha, William Cairns, Catherine E. Clarke, Gareth J. Sanger, Owen Jenkins, John B. Davis, Philip David Hayes
Publikováno v:
Pain. 88:205-215
Capsaicin, resiniferatoxin, protons or heat have been shown to activate an ion channel, termed the rat vanilloid receptor-1 (rVR1), originally isolated by expression cloning for a capsaicin sensitive phenotype. Here we describe the cloning of a human
Autor:
Andrew D. Randall, David A. Campbell, Malcolm Duckworth, Paul R. Murdock, Helen J. Meadows, Conrad Gerald Chapman, Rosemary E. Kelsell, Gillian I. Rennie, Israel S. Gloger, Rob J. Godden
Publikováno v:
Molecular Brain Research. 82:74-83
We have isolated, by degenerate PCR, a complementary DNA encoding a novel two pore domain potassium channel. This is the 7th functional member of the human tandem pore domain potassium channel family to be reported. It has an open reading frame of 1.
Publikováno v:
The Journal of Physiology. 523:697-703
1. Effects of external pH on the human P2X4 purinoceptor, an ATP-activated ion channel, were studied using the Xenopus oocyte expression system. 2. Changing the external pH from 7.4 to 6.5 significantly reduced, whilst an increase to pH 8 enhanced, m
Autor:
David O. Carpenter, Gayle Chapman, Jackie Meakin, Catherine E. Clarke, Simon Q. J. Rice, Helen J. Meadows, Stephen J. Brough, Gareth J. Sanger, David C. Harrison, W.Jeff Tomlinson, Robert P. Davis, Martyn D. Wood, Martyn C. Coldwell, Mark Thomas Mchale
Publikováno v:
Neuroscience Letters. 273:183-186
P2X 4 receptors are expressed in specific brain areas. We now describe site-specific splice variations of the human P2X 4 receptor subunit, occurring at residue [YVI G ↓WVFV(W)] near the end of the first predicted transmembrane domain. p2x 4(b) is