2003
Calmodulin Binds to the C Terminus of Sodium Channels Nav1.4 and Nav1.6 and Differentially Modulates Their Functional Properties
Herzog RI, Liu C, Waxman SG, Cummins TR. Calmodulin Binds to the C Terminus of Sodium Channels Nav1.4 and Nav1.6 and Differentially Modulates Their Functional Properties. Journal Of Neuroscience 2003, 23: 8261-8270. PMID: 12967988, PMCID: PMC6740705, DOI: 10.1523/jneurosci.23-23-08261.2003.Peer-Reviewed Original ResearchConceptsVoltage-gated sodium channelsSodium channelsNeuronal sodium channelsCalcium-independent mechanismVGSC isoformsNeuronal plasticityCell excitabilityNav1.6 channelsNav1.6Overexpression of CaMCalcium-dependent mannerCalcium-independent mannerNav1.4Sodium channel Nav1.4Channel Nav1.4Functional expressionCurrent amplitude
2001
Diverse Functions and Dynamic Expression of Neuronal Sodium Channels
Waxman SG, Cummins TR, Black JA, Dib‐Hajj S. Diverse Functions and Dynamic Expression of Neuronal Sodium Channels. Novartis Foundation Symposia 2001, 241: 34-60. PMID: 11771649, DOI: 10.1002/0470846682.ch4.Peer-Reviewed Reviews, Practice Guidelines, Standards, and Consensus StatementsConceptsChannel gene expressionNervous systemChannel expressionNormal nervous systemTypes of neuronsNeuronal sodium channelsChannel genesChronic painGene expressionMultiple sclerosisPeripheral axonsChannel subtypesMaladaptive changesPathological neuronsNeuronal functionPurkinje cellsTherapeutic opportunitiesExperimental modelAmino acid sequenceSodium channelsNa channelsNeuronsDifferent amino acid sequencesRecent evidenceSelective modulators
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