Abstract
Recent papers have described glutamine to arginine point mutations of the cloned AMPA/Kainate receptor subunits that alter current-voltage relationship and suppress Ca2+ permeability, thus linking these two characteristics. We describe a glutamine to histidine mutation at the same position, which alters current-voltage relationship but retains Ca2+ permeability, thus dissociating the two properties.
MeSH terms
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Animals
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Barium / pharmacology
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Base Sequence
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Calcium / metabolism*
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Calcium Channels / drug effects
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Calcium Channels / physiology*
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Cloning, Molecular
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Evoked Potentials / drug effects
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Glutamates / metabolism*
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Glutamine*
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Histidine*
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Ibotenic Acid / analogs & derivatives
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Ibotenic Acid / pharmacology
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Kainic Acid / pharmacology
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Macromolecular Substances
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Molecular Sequence Data
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Mutagenesis, Site-Directed*
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Oligodeoxyribonucleotides
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Oocytes / drug effects
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Oocytes / physiology*
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Plasmids
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Quinoxalines / pharmacology
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Receptors, Glutamate
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Receptors, Neurotransmitter / genetics
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Receptors, Neurotransmitter / metabolism
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Receptors, Neurotransmitter / physiology*
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Transcription, Genetic
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Xenopus laevis
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alpha-Amino-3-hydroxy-5-methyl-4-isoxazolepropionic Acid
Substances
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Calcium Channels
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Glutamates
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Macromolecular Substances
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Oligodeoxyribonucleotides
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Quinoxalines
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Receptors, Glutamate
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Receptors, Neurotransmitter
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Glutamine
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Barium
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Ibotenic Acid
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Histidine
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FG 9041
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alpha-Amino-3-hydroxy-5-methyl-4-isoxazolepropionic Acid
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Kainic Acid
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Calcium