Time-resolved photolabeling by quinacrine azide of a noncompetitive inhibitor site of the nicotinic acetylcholine receptor in a transient, agonist-induced state.
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
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1. Conformational Changes in the Nicotinic Acetylcholine Receptor during Gating and Desensitization;Biochemistry;2009-12-14
2. Dynamic Structural Investigations on the Torpedo Nicotinic Acetylcholine Receptor by Time-Resolved Photoaffinity Labeling;ChemBioChem;2006-03-15
3. Gating-enhanced Accessibility of Hydrophobic Sites within the Transmembrane Region of the Nicotinic Acetylcholine Receptor's δ-Subunit;Journal of Biological Chemistry;2005-04
4. Structural effects of quinacrine binding in the open channel of the acetylcholine receptor;Proceedings of the National Academy of Sciences;2003-03-18
5. Emerging structure of the Nicotinic Acetylcholine receptors;Nature Reviews Neuroscience;2002-02
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