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- W2017161867 abstract "Voltage-gated sodium channels mediate inward current of action potentials upon membrane depolarization of excitable cells. The initial transient sodium current is restricted to milliseconds through three distinct channel-inactivating and blocking mechanisms. All pore-forming alpha subunits of sodium channels possess structural elements mediating fast inactivation upon depolarization and recovery within milliseconds upon membrane repolarization. Accessory subunits modulate fast inactivation dynamics, but these proteins can also limit current by contributing distinct inactivation and blocking particles. A-type isoforms of fibroblast growth factor homologous factors (FHFs) bear a particle that induces long-term channel inactivation, while sodium channel subunit Navβ4 employs a blocking particle that rapidly dissociates upon membrane repolarization to generate resurgent current. Despite their different physiological functions, the FHF and Navβ4 particles have similarity in amino acid composition and mechanisms for docking within sodium channels. The three competing channel-inactivating and blocking processes functionally interact to regulate a neuron’s intrinsic excitability." @default.
- W2017161867 created "2016-06-24" @default.
- W2017161867 creator A5009400432 @default.
- W2017161867 date "2011-09-27" @default.
- W2017161867 modified "2023-10-06" @default.
- W2017161867 title "Voltage-gated sodium channel-associated proteins and alternative mechanisms of inactivation and block" @default.
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- W2017161867 doi "https://doi.org/10.1007/s00018-011-0832-1" @default.
- W2017161867 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3272111" @default.
- W2017161867 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/21947499" @default.
- W2017161867 hasPublicationYear "2011" @default.
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