Crotonic Acid Blocks the Gloeobacter Ligand-Gated Ion Channel (GLIC) via the Extracellular 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.6b00531
Reference20 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. Structural basis for ion permeation mechanism in pentameric ligand-gated ion channels
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. Short‐chain mono‐carboxylates as negative modulators of allosteric transitions in Gloeobacter violaceus ligand‐gated ion channel, and impact of a pre‐β5 strand (Loop Ω) double mutation on crotonate, not butyrate effect;Physiological Reports;2024-02
2. Fumarate as positive modulator of allosteric transitions in the pentameric ligand‐gated ion channel GLIC: requirement of an intact vestibular pocket;The Journal of Physiology;2023-04-27
3. Short-chain mono-carboxylates as negative modulators of allosteric transitions in GLIC, and impact of a pre-β5 strand (Loop Ω) double mutation on crotonate, not butyrate effect;2023-03-15
4. Structural evidence for the binding of monocarboxylates and dicarboxylates at pharmacologically relevant extracellular sites of a pentameric ligand-gated ion channel;Acta Crystallographica Section D Structural Biology;2020-06-30
5. Characterization of the dynamic resting state of a pentameric ligand-gated ion channel by cryo-electron microscopy and simulations;2020-06-20
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