1995
Hypertension caused by a truncated epithelial sodium channel γ subunit: genetic heterogeneity of Liddle syndrome
Hansson J, Nelson-Williams C, Suzuki H, Schild L, Shimkets R, Lu Y, Canessa C, Iwasaki T, Rossier B, Lifton R. Hypertension caused by a truncated epithelial sodium channel γ subunit: genetic heterogeneity of Liddle syndrome. Nature Genetics 1995, 11: 76-82. PMID: 7550319, DOI: 10.1038/ng0995-76.Peer-Reviewed Original ResearchMeSH KeywordsAdolescentAdultAldosteroneAllelesAmino Acid SequenceAnimalsBase SequenceCodonEpithelial Sodium ChannelsGene Expression RegulationGenesGenes, DominantHumansHypertensionHypokalemiaIon Channel GatingKidney Tubules, ProximalMiddle AgedMolecular Sequence DataMutagenesis, Site-DirectedMutationOocytesPedigreeRatsRecombinant Fusion ProteinsReninSequence AlignmentSequence Homology, Amino AcidSodium ChannelsSodium, DietarySyndromeTerminator Regions, GeneticXenopus laevisConceptsLiddle's syndromeRenal epithelial sodium channelEpithelial Sodium Channel γ-SubunitSalt-sensitive formsChannel activityChannel γ subunitBlood pressureDietary saltEpithelial sodium channelHuman hypertensionSyndromeGenetic heterogeneityHypertensionSodium channelsIndependent roleConstitutive activationΓ subunitMendelian disordersNegative regulationMutations
1994
Membrane topology of the epithelial sodium channel in intact cells
Canessa C, Merillat A, Rossier B. Membrane topology of the epithelial sodium channel in intact cells. American Journal Of Physiology 1994, 267: c1682-c1690. PMID: 7810611, DOI: 10.1152/ajpcell.1994.267.6.c1682.Peer-Reviewed Original ResearchMeSH KeywordsAmilorideAnimalsCell MembraneCytoskeletonDogsGlycosylationMutagenesis, Site-DirectedRabbitsSodium ChannelsStructure-Activity RelationshipXenopus laevisConceptsLarge hydrophilic loopHydrophilic loopIntact cellsMembrane topologyEpithelial sodium channelPutative transmembrane domainsStop-transfer signalAmiloride-sensitive epithelial sodium channelCell-free translation assaysShort NH2Transmembrane domainMembrane insertionHomologous subunitsXenopus laevis oocytesTranslation assaysSodium channelsGlycosylation sitesCOOH terminusCytoplasmic sideFunctional expressionTerminal endSubunitsHydrophilic NH2Laevis oocytesAlpha-rENaC
1993
Mutation of a tyrosine in the H3-H4 ectodomain of Na,K-ATPase alpha subunit confers ouabain resistance.
Canessa C, Horisberger J, Rossier B. Mutation of a tyrosine in the H3-H4 ectodomain of Na,K-ATPase alpha subunit confers ouabain resistance. Journal Of Biological Chemistry 1993, 268: 17722-17726. PMID: 8394348, DOI: 10.1016/s0021-9258(17)46764-0.Peer-Reviewed Original ResearchAmino Acid SequenceAnimalsBase SequenceBinding SitesCell LineCloning, MolecularDogsFemaleKidneyKineticsMacromolecular SubstancesMolecular Sequence DataMutagenesis, Site-DirectedOligodeoxyribonucleotidesOocytesOuabainPeptide FragmentsPolymerase Chain ReactionProtein ConformationRecombinant ProteinsSequence Homology, Amino AcidSodium-Potassium-Exchanging ATPaseTime FactorsXenopus laevis