2015
Receptors and Transduction Mechanisms I: Receptors Coupled Directly to Ion Channels
Levitan I, Kaczmarek L. Receptors and Transduction Mechanisms I: Receptors Coupled Directly to Ion Channels. 2015, 239-262. DOI: 10.1093/med/9780199773893.003.0011.Chapters
2001
Ion Channels Are Membrane Proteins
B.Levitan I, Kaczmarek L. Ion Channels Are Membrane Proteins. 2001, 89-112. DOI: 10.1093/oso/9780195145236.003.0005.Peer-Reviewed Original ResearchIon channelsSingle ion channelsIon channel structureAmino acid sequenceMolecular cloning techniquesMembrane proteinsAcid sequenceSuch measurementsCloning techniquesNovel insightsProtein moleculesMacroscopic membrane currentsKey functional propertiesChannel structureFunctional propertiesPowerful combinationProteinChannelsActivity of populationsMoleculesSequenceMembrane currentsStructural approachActivityMeasurements
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