Conotoxin MI inhibits the α–δ acetylcholine binding site of the Torpedo marmorata receptor
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry,Biophysics
Reference20 articles.
1. The α-conotoxins GI and MI distinguish between the nicotinic acetylcholine receptor agonist sites while SI does not;Hann;Biochemistry,1994
2. α-Conotoxin selectively inhibits one of the two acetylcholine binding sites of nicotinic receptors;Groebe;Mol. Pharmacol.,1995
3. Glycosylation sites selectively interfere with alpha-toxin binding to the nicotinic acetylcholine receptor;Kreienkamp;J. Biol. Chem.,1994
4. α-Conotoxins, small peptide probes of nicotinic acetylcholine receptors;Myers;Biochemistry,1991
5. Alpha-Conotoxin EI, a new nicotinic acetylcholine receptor antagonist with novel selectivity;Martinez;Biochemistry,1995
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1. Two Potent ?3/5 Conotoxins from Piscivorous Conus achatinus;Acta Biochimica et Biophysica Sinica;2007-06
2. Interactions between α-conotoxin MI and the Torpedo marmorata receptor α–δ interface;Biochemical and Biophysical Research Communications;2007-03
3. Natural α-conotoxins and their synthetic analogues in study of nicotinic acetylcholine receptors;Russian Journal of Bioorganic Chemistry;2006-03
4. Drugs from the Sea: Conopeptides as Potential Therapeutics;Current Medicinal Chemistry;2004-07-01
5. Physico-chemical characterization and synthesis of neuronally active alpha-conotoxins;European Journal of Biochemistry;2004-06
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