2005 Journal Article Identification of molluscan nicotinic acetylcholine receptor (nAChR) subunits involved in formation of cation- and anion-selective nAChRsvan Nierop, Pim, Keramidas, Angelo, Bertrand, Sonia, van Minnen, Jan, Gouwenberg, Yvonne, Bertrand, Daniel and Smit, August B. (2005). Identification of molluscan nicotinic acetylcholine receptor (nAChR) subunits involved in formation of cation- and anion-selective nAChRs. Journal of Neuroscience, 25 (46), 10617-10626. doi: 10.1523/JNEUROSCI.2015-05.2005 |
2004 Journal Article Ligand-gated ion channels: Mechanisms underlying ion selectivityKeramidas, Angelo, Moorhouse, Andrew J., Schofield, Peter R. and Barry, Peter H. (2004). Ligand-gated ion channels: Mechanisms underlying ion selectivity. Progress in Biophysics and Molecular Biology, 86 (2), 161-204. doi: 10.1016/j.pbiomolbio.2003.09.002 |
2003 Journal Article The contribution of proline 250 (P-2’) to pore diameter and ion selectivity in the human glycine receptor channelLee, David J.-S., Keramidas, Angelo, Moorhouse, Andrew J., Schofield, Peter R. and Barry, Peter H. (2003). The contribution of proline 250 (P-2’) to pore diameter and ion selectivity in the human glycine receptor channel. Neuroscience Letters, 351 (3), 196-200. doi: 10.1016/S0304-3940(03)00977-7 |
2003 Journal Article The contribution of proline 250 (P-2 ') to pore diameter and ion selectivity in the human glycine receptor channelLee, DJS, Keramidas, A, Moorhouse, AJ, Schofield, PR and Barry, PH (2003). The contribution of proline 250 (P-2 ') to pore diameter and ion selectivity in the human glycine receptor channel. Neuroscience Letters, 351 (3), 196-200. doi: 10.1016/S0304-3940(03)00977-7 |
2003 Conference Publication Mechanism of ion permeation in the glycine receptor and its cation-selective mutationsO'Mara, Megan, Keramidas, Angelo, Barry, Peter H. and Chung, Shin-Ho (2003). Mechanism of ion permeation in the glycine receptor and its cation-selective mutations. 47th Annual Meeting of the Biophysical Society, San Antonio, Texas, 1-5 March 2003. Bethesda, MD, U.S.A.: Cell Press for the Biophysical Society. |
2003 Conference Publication Mechanism of ion permeation in the glycine receptor and its cation-selective mutationsO'Mara, M., Keramidas, A., Barry, P. H. and Chung, S. H. (2003). Mechanism of ion permeation in the glycine receptor and its cation-selective mutations. 47th Annual Meeting of the Biophysical-Society, San Antonio Texas, 1-5 March 2003. Bethesda, MD United States: Biophysical Society. |
2002 Journal Article Single channel analysis of conductance and rectification in cation-selective, mutant glycine receptor channelsMoorhouse, Andrew J., Keramidas, Angelo, Zaykin, Andrey, Schofield, Peter R. and Barry, Peter H. (2002). Single channel analysis of conductance and rectification in cation-selective, mutant glycine receptor channels. Journal of General Physiology, 119 (5), 411-425. doi: 10.1085/jgp.20028553 |
2002 Journal Article Cation-selective mutations in the M2 domain of the inhibitory glycine receptor channel reveal determinants of ion-charge selectivityKeramidas, Angelo, Moorhouse, Andrew J., Pierce, Kerrie D. and Schofield, Peter R. (2002). Cation-selective mutations in the M2 domain of the inhibitory glycine receptor channel reveal determinants of ion-charge selectivity. Journal of General Physiology, 119 (5), 393-410. doi: 10.1085/jgp.20028552 |
2000 Journal Article M2 pore mutations convert the glycine receptor channel from being anion- to cation-selectiveKeramidas, A, Moorhouse, AJ, French, CR, Schofield, PR and Barry, PH (2000). M2 pore mutations convert the glycine receptor channel from being anion- to cation-selective. Biophysical Journal, 79 (1), 247-259. doi: 10.1016/S0006-3495(00)76287-4 |
1999 Journal Article Measurement of the limiting equivalent conductivities and mobilities of the most prevalent ionic species of EGTA (EGTA2- and EGTA3-) for use in electrophysiological experimentsKeramidas, Angelo , Barry, Peter H., Moorhouse, Andrew and Kuhlmann, Levin (1999). Measurement of the limiting equivalent conductivities and mobilities of the most prevalent ionic species of EGTA (EGTA2- and EGTA3-) for use in electrophysiological experiments. Journal of Neuroscience Methods, 89 (1), 41-47. doi: 10.1016/S0165-0270(99)00036-9 |