Nature of the 5? residue in the M2 domain affects function of the human ?1?1 GABAA receptor
- 1 July 1997
- Vol. 26 (3) , 324-327
- https://doi.org/10.1002/(sici)1098-2396(199707)26:3<324::aid-syn13>3.0.co;2-v
Abstract
No abstract availableKeywords
This publication has 15 references indexed in Scilit:
- Toward a structural basis for the function of nicotinic acetylcholine receptors and their cousinsNeuron, 1995
- Rapid desensitization of ?1?1 GABAA receptors expressed in Sf9 cells under optimized conditionsThe Journal of Membrane Biology, 1995
- Channel gating governed symmetrically by conserved leucine residues in the M2 domain of nicotinic receptorsNature, 1995
- Acceleration of GABA-dependent desensitization by mutating threonine 266 to alanine of the α6 subunit of rat GABAA receptorsNeuroscience Letters, 1995
- A unique amino acid of the Drosophila GABA receptor with influence on drug sensitivity by two mechanisms.The Journal of Physiology, 1994
- Mutations at two distinct sites within the channel domain M2 alter calcium permeability of neuronal alpha 7 nicotinic receptor.Proceedings of the National Academy of Sciences, 1993
- Genetic manipulation of ion channels: A new approach to structure and mechanismNeuron, 1989
- Evidence That the M2 Membrane-Spanning Region Lines the Ion Channel Pore of the Nicotinic ReceptorScience, 1988
- Location of a δ-subunit region determining ion transport through the acetylcholine receptor channelNature, 1986
- Improved patch-clamp techniques for high-resolution current recording from cells and cell-free membrane patchesPflügers Archiv - European Journal of Physiology, 1981