Design, synthesis and functional characterization of a pentameric channel protein that mimics the presumed pore structure of the nicotinic cholinergic receptor
- 12 April 1993
- journal article
- Published by Wiley in FEBS Letters
- Vol. 320 (3) , 261-266
- https://doi.org/10.1016/0014-5793(93)80599-p
Abstract
No abstract availableKeywords
This publication has 31 references indexed in Scilit:
- Neurotransmitter action: Opening of ligand-gated ion channelsCell, 1993
- The functional architecture of the acetylcholine nicotinic receptor explored by affinity labelling and site-directed mutagenesisQuarterly Reviews of Biophysics, 1992
- Three-dimensional structure of the acetylcholine receptor by cryoelectron microscopy and helical image reconstruction.The Journal of cell biology, 1990
- Bundles of amphipathic transmembrane α‐helices as a structural motif for ion‐conducting channel proteins: Studies on sodium channels and acetylcholine receptorsProteins-Structure Function and Bioinformatics, 1990
- M2 delta, a candidate for the structure lining the ionic channel of the nicotinic cholinergic receptor.Proceedings of the National Academy of Sciences, 1988
- The ion channel of the nicotinic acetylcholine receptor is formed by the homologous helices M II of the receptor subunitsFEBS Letters, 1986
- Structure of the high-affinity binding site for noncompetitive blockers of the acetylcholine receptor: serine-262 of the delta subunit is labeled by [3H]chlorpromazine.Proceedings of the National Academy of Sciences, 1986
- The permeability of endplate channels to monovalent and divalent metal cations.The Journal of general physiology, 1980
- The permeability of the endplate channel to organic cations in frog muscle.The Journal of general physiology, 1980
- Molecular weight in detergent solution of acetylcholine receptor from Torpedo californicaBiochemistry, 1978