Coupled Proteolytic and Mass Spectrometry Studies Indicate a Novel Topology for the Glycine Receptor
Open Access
- 1 May 2000
- journal article
- Published by Elsevier
- Vol. 275 (18) , 13683-13689
- https://doi.org/10.1074/jbc.275.18.13683
Abstract
No abstract availableKeywords
This publication has 26 references indexed in Scilit:
- Structure of bacteriorhodopsin at 1.55 Å resolutionJournal of Molecular Biology, 1999
- Improved Secondary Structure Predictions for a Nicotinic Receptor Subunit: Incorporation of Solvent Accessibility and Experimental Data into a Two-Dimensional RepresentationBiophysical Journal, 1999
- Electron-crystallographic Refinement of the Structure of BacteriorhodopsinJournal of Molecular Biology, 1996
- Toward a structural basis for the function of nicotinic acetylcholine receptors and their cousinsNeuron, 1995
- Acetylcholine receptor channel imaged in the open stateNature, 1995
- Ligand-gated ion channels in the brain: The amino acid receptor superfamilyNeuron, 1990
- Functional chloride channels by mammalian cell expression of rat glycine receptor subunitNeuron, 1989
- Topography of surface-exposed amino acids in the membrane protein bacteriorhodopsin determined by proteolysis and micro-sequencingBiochimica et Biophysica Acta (BBA) - Biomembranes, 1989
- Conserved quaternary structure of ligand-gated ion channels: the postsynaptic glycine receptor is a pentamer.Proceedings of the National Academy of Sciences, 1988
- Stability of transmembrane regions in bacteriorhodopsin studied by progressive proteolysisThe Journal of Membrane Biology, 1985