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
1990
Estrogen induction of a small, putative K+ channel mRNA in rat uterus
Pragnell M, Snay K, Trimmer J, MacLusky N, Naftolin F, Kaczmarek L, Boyle M. Estrogen induction of a small, putative K+ channel mRNA in rat uterus. Neuron 1990, 4: 807-812. PMID: 2344412, DOI: 10.1016/0896-6273(90)90207-v.Peer-Reviewed Original ResearchConceptsMRNA speciesAmino acid proteinProkaryotic ion channelsDramatic long-term changesMolecular cloningAcid proteinIon channel expressionMammalian sourcesIon channelsXenopus oocytesVoltage-dependent channelsSpeciesStructural motifsCritical roleChannel expressionMRNAChannel mRNAEstrogen inductionLong-term changesInductionCloningProteinMotifRegulationOocytes