The Proton Responsiveness in the Extracellular Domain of GLIC Differs in the Presence of the ELIC Transmembrane Domain
Author:
Affiliation:
1. Department of Biochemistry, University of Cambridge, Cambridge CB2 1QW, U.K.
Funder
Medical Research Council
Cambridge Commonwealth, European and International Trust
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
http://pubs.acs.org/doi/pdf/10.1021/acs.biochem.6b00900
Reference24 articles.
1. X-ray structure of a pentameric ligand-gated ion channel in an apparently open conformation
2. Structure of a potentially open state of a proton-activated pentameric ligand-gated ion channel
3. Crystal structures of a pentameric ligand-gated ion channel provide a mechanism for activation
4. Gating of the proton-gated ion channel from Gloeobacter violaceus at pH 4 as revealed by X-ray crystallography
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1. Full mutational mapping of titratable residues helps to identify proton-sensors involved in the control of channel gating in the Gloeobacter violaceus pentameric ligand-gated ion channel;PLOS Biology;2017-12-27
2. A chimeric prokaryotic-eukaryotic pentameric ligand gated ion channel reveals interactions between the extracellular and transmembrane domains shape neurosteroid modulation;Neuropharmacology;2017-10
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