Nonequivalence of .alpha.-bungarotoxin binding sites in the native nicotinic receptor molecule
Author:
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi00456a029
Reference68 articles.
1. Interaction of [125I]-.alpha.-bungarotoxin with acetylcholine receptor from Torpedo californica
2. Image analysis of the heavy form of the acetylcholine receptor from Torpedo marmorata
3. Desensitization of membrane-bound Torpedo acetylcholine receptor by amine noncompetitive antagonists and aliphatic alcohols: studies of [3H]acetylcholine binding and sodium-22 ion fluxes
4. An immunochemical approach to the identification of the MBTA binding site of the nicotinic acetylcholine receptor of Torpedocalifornica
5. Long-lived metastable state and hysteresis in the binding of acetylcholine to Torpedo californica acetylcholine receptor
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1. Role of amino and carboxyl groups of cobrotoxin in the conformational stability and the interaction with acetylcholine receptor;International Journal of Peptide and Protein Research;2009-01-12
2. Electron microscopic evidence for nucleation and growth of 3D acetylcholine receptor microcrystals in structured lipid-detergent matrices;Proceedings of the National Academy of Sciences;2003-09-17
3. Muscarinic Toxin-Like Proteins from Taiwan Banded Krait (Bungarus multicinctus) Venom: Purification, Characterization and Gene Organization;Biological Chemistry;2002-09-17
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