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      International Union of Pharmacology. XLVII. Nomenclature and Structure-Function Relationships of Voltage-Gated Sodium Channels

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      Pharmacological Reviews
      American Society for Pharmacology & Experimental Therapeutics (ASPET)

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          Abstract

          The family of voltage-gated sodium channels initiates action potentials in all types of excitable cells. Nine members of the voltage-gated sodium channel family have been characterized in mammals, and a 10th member has been recognized as a related protein. These distinct sodium channels have similar structural and functional properties, but they initiate action potentials in different cell types and have distinct regulatory and pharmacological properties. This article presents the molecular relationships and physiological roles of these sodium channel proteins and provides comprehensive information on their molecular, genetic, physiological, and pharmacological properties.

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          International Union of Pharmacology. XLVIII. Nomenclature and structure-function relationships of voltage-gated calcium channels.

          The family of voltage-gated calcium channels serves as the key transducers of cell surface membrane potential changes into local intracellular calcium transients that initiate many different physiological events. There are 10 members of the voltage-gated calcium channel family that have been characterized in mammals, and they serve distinct roles in cellular signal transduction. This article presents the molecular relationships and physiological functions of these calcium channel proteins and provides comprehensive information on their molecular, genetic, physiological, and pharmacological properties.
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            Author and article information

            Journal
            Pharmacological Reviews
            Pharmacol Rev
            American Society for Pharmacology & Experimental Therapeutics (ASPET)
            0031-6997
            1521-0081
            December 28 2005
            December 2005
            December 2005
            December 28 2005
            : 57
            : 4
            : 397-409
            Article
            10.1124/pr.57.4.4
            16382098
            ace5d586-4aec-49cd-b277-3a8875acc4c4
            © 2005
            History

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