2014
More Than a Pore: Ion Channel Signaling Complexes
Lee A, Fakler B, Kaczmarek LK, Isom LL. More Than a Pore: Ion Channel Signaling Complexes. Journal Of Neuroscience 2014, 34: 15159-15169. PMID: 25392484, PMCID: PMC4228125, DOI: 10.1523/jneurosci.3275-14.2014.Peer-Reviewed Original ResearchConceptsIon channelsHeterologous expression systemIon channel complexSignaling ComplexFunctional dissectionHuman genomeMolecular basisExpression systemSecond messengerHuman diseasesChannel complexCellular excitabilityProteinNew insightsSuch interactionsInteractomeGenomeUnexpected propertiesComplexesMessengerPathwayInteractionDysregulationLocalizationVivo
2001
Title Pages
B.Levitan I, Kaczmarek L. Title Pages. 2001, i-iv. DOI: 10.1093/oso/9780195145236.002.0001.Peer-Reviewed Original ResearchElectrical activityAppropriate synaptic connectionsAction of neurotransmittersBiochemical pathwaysMolecular mechanismsMolecular biologyUndifferentiated cellsIon channelsCellular propertiesSynaptic connectionsNerve cellsNeuronsSensory cellsSynaptic junctionsMolecular factorsSingle neuronsFirst courseCellsGenomeBiologyVaried patternsNeurotransmittersHormoneSecretionActivityPreface
B.Levitan I, Kaczmarek L. Preface. 2001, vii-viii. DOI: 10.1093/oso/9780195145236.002.0003.Peer-Reviewed Original ResearchElectrical activityBiochemical pathwaysMolecular mechanismsAppropriate synaptic connectionsMolecular biologyUndifferentiated cellsAction of neurotransmittersIon channelsCellular propertiesSensory cellsMolecular factorsSynaptic connectionsNerve cellsNeuronsSynaptic junctionsSingle neuronsCellsFirst courseGenomeBiologyPathwayActivityMechanismVaried patternsAccount of mechanismsPreface to the Second Edition
B.Levitan I, Kaczmarek L. Preface to the Second Edition. 2001, ix-x. DOI: 10.1093/oso/9780195145236.002.0004.Peer-Reviewed Original ResearchElectrical activityAppropriate synaptic connectionsBiochemical pathwaysAction of neurotransmittersMolecular mechanismsMolecular biologyUndifferentiated cellsIon channelsCellular propertiesSensory cellsMolecular factorsSynaptic connectionsNerve cellsNeuronsSynaptic junctionsSingle neuronsCellsFirst courseGenomeBiologyPathwayVaried patternsActivityMechanismNeurotransmittersPreface to the First Edition
B.Levitan I, Kaczmarek L. Preface to the First Edition. 2001, xi-xii. DOI: 10.1093/oso/9780195145236.002.0005.Peer-Reviewed Original ResearchElectrical activityBiochemical pathwaysMolecular mechanismsAppropriate synaptic connectionsAction of neurotransmittersMolecular biologyUndifferentiated cellsIon channelsCellular propertiesSensory cellsMolecular factorsSynaptic connectionsNerve cellsNeuronsSynaptic junctionsSingle neuronsCellsFirst courseGenomeBiologyPathwayActivityMechanismVaried patternsNeurotransmittersLearning and Memory
B.Levitan I, Kaczmarek L. Learning and Memory. 2001, 537-570. DOI: 10.1093/oso/9780195145236.003.0020.Peer-Reviewed Original Research
1995
A new family of outwardly rectifying potassium channel proteins with two pore domains in tandem
Ketchum K, Joiner W, Sellers A, Kaczmarek L, Goldstein S. A new family of outwardly rectifying potassium channel proteins with two pore domains in tandem. Nature 1995, 376: 690-695. PMID: 7651518, DOI: 10.1038/376690a0.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBase SequenceCaenorhabditis elegansCells, CulturedDNA PrimersDrosophilaMolecular Sequence DataOocytesPatch-Clamp TechniquesPotassiumPotassium ChannelsProtein ConformationRecombinant ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSequence Homology, Amino AcidSodiumXenopus laevisConceptsP domainPotassium channel proteinCaenorhabditis elegansCommon structural motifChannel proteinsPore domainCellular membranesPrimary structureExcised membrane patchesSignature sequencesFlow of ionsAmino acidsXenopus laevisSelective currentMembrane potentialStructural motifsMembrane patchesPotassium channelsExternal divalent cationsDivalent cationsFunctional propertiesElegansVoltage-dependent mannerGenomeDomain