Site-directed disulfide reduction using an affinity reagent: Application on the nicotinic acetylcholine receptor
Author:
Publisher
Wiley
Subject
Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1016/0014-5793(95)00116-Q/fullpdf
Reference23 articles.
1. Identification of the alpha subunit half-cystine specifically labeled by an affinity reagent for the acetylcholine receptor binding site.
2. Acetylcholine receptor binding site contains a disulfide cross-link between adjacent half-cystinyl residues.
3. Bromoacetylcholine as an affinity label of the acetylcholine receptor from Torpedo californica
4. Stoichiometry of the Ligand-Binding Sites in the Acetylcholine-Receptor Oligomer from Muscle and from Electric Organ. Measurement by Affinity Alkylation with Bromoacetylcholine
5. A high-affinity site for acetylcholine occurs close to the .alpha.-.gamma. subunit interface of Torpedo nicotinic acetylcholine receptor
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1. A Potent, Versatile Disulfide-Reducing Agent from Aspartic Acid;Journal of the American Chemical Society;2012-02-21
2. Mitochondria, oxidative stress, and temporal lobe epilepsy;Epilepsy Research;2010-01
3. Acid sensing ionic channels: Modulation by redox reagents;Biochimica et Biophysica Acta (BBA) - Molecular Cell Research;2005-08
4. Localization of agonist and competitive antagonist binding sites on nicotinic acetylcholine receptors;Neurochemistry International;2000-06
5. Modulation of neuronal and recombinant GABA A receptors by redox reagents;The Journal of Physiology;1999-05
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