Abstract
Recent chemical and advanced structural studies on site-directed and naturally occurring pathological mutants of individual members of the multigene family of nicotinic acetylcholine receptors have yielded structure-function relationships supporting indirect 'allosteric' interactions between the acetylcholine-binding sites and the ion channel in signal transduction.
Publication types
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Research Support, Non-U.S. Gov't
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Review
MeSH terms
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Allosteric Regulation
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Allosteric Site
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Animals
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Binding Sites
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Brain / physiology
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Caenorhabditis elegans / physiology
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Consciousness Disorders / metabolism
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Forecasting
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Helminth Proteins / chemistry
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Helminth Proteins / physiology
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Humans
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Mice
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Mice, Knockout
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Mice, Transgenic
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Models, Animal
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Nerve Tissue Proteins / chemistry
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Nerve Tissue Proteins / physiology*
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Nicotinic Agonists / pharmacology
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Nicotinic Antagonists / pharmacology
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Protein Conformation
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Protein Subunits
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Receptors, Nicotinic / chemistry
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Receptors, Nicotinic / physiology*
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Signal Transduction / physiology*
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Smoking / metabolism
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Structure-Activity Relationship
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Torpedo / physiology
Substances
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Helminth Proteins
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Nerve Tissue Proteins
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Nicotinic Agonists
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Nicotinic Antagonists
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Protein Subunits
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Receptors, Nicotinic