The strychnine-binding subunit of the glycine receptor shows homology with nicotinic acetylcholine receptors
- 16 July 1987
- journal article
- research article
- Published by Springer Nature in Nature
- Vol. 328 (6127) , 215-220
- https://doi.org/10.1038/328215a0
Abstract
We have cloned and sequenced cDNAs of the strychnine-binding subunit of the rat glycine receptor, a neurotransmitter-gated chloride channel protein of the CNS. The deduced polypeptide shows significant structural and amino-acid sequence homology with nicotinic acetylcholine receptor proteins, indicating that there is a family of genes encoding neurotransmitter-gated ion channels.Keywords
This publication has 34 references indexed in Scilit:
- Solubilization of the glycine receptor from rat spinal cordBrain Research, 1981
- UV light-induced cross-linking of strychnine to the glycine receptor of rat spinal cord membranesBiochemical and Biophysical Research Communications, 1981
- A gas-liquid solid phase peptide and protein sequenator.Journal of Biological Chemistry, 1981
- Postnatal Development of Synaptic Glycine Receptors in Normal and Hyperglycinemic RatsJournal of Neurochemistry, 1981
- Prediction of protein antigenic determinants from amino acid sequences.Proceedings of the National Academy of Sciences, 1981
- Hybridization of denatured RNA and small DNA fragments transferred to nitrocellulose.Proceedings of the National Academy of Sciences, 1980
- Glycine and experimental spinal spasticityNeurology, 1979
- DNA sequencing with chain-terminating inhibitorsProceedings of the National Academy of Sciences, 1977
- Peptide mapping by limited proteolysis in sodium dodecyl sulfate and analysis by gel electrophoresis.Journal of Biological Chemistry, 1977
- The specific ionic conductances and the ionic movements across the motoneuronal membrane that produce the inhibitory post‐synaptic potentialThe Journal of Physiology, 1955