2016
Romk1 Knockout Mice Do Not Produce Bartter Phenotype but Exhibit Impaired K Excretion*
Dong K, Yan Q, Lu M, Wan L, Hu H, Guo J, Boulpaep E, Wang W, Giebisch G, Hebert SC, Wang T. Romk1 Knockout Mice Do Not Produce Bartter Phenotype but Exhibit Impaired K Excretion*. Journal Of Biological Chemistry 2016, 291: 5259-5269. PMID: 26728465, PMCID: PMC4777858, DOI: 10.1074/jbc.m115.707877.Peer-Reviewed Original Research
2005
Requirement of Voltage-Gated Calcium Channel ß4 Subunit for T Lymphocyte Functions
Badou A, Basavappa S, Desai R, Peng YQ, Matza D, Mehal WZ, Kaczmarek LK, Boulpaep EL, Flavell RA. Requirement of Voltage-Gated Calcium Channel ß4 Subunit for T Lymphocyte Functions. Science 2005, 307: 117-121. PMID: 15637280, DOI: 10.1126/science.1100582.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCalciumCalcium Channels, L-TypeCalcium SignalingCD4-Positive T-LymphocytesCytokinesDNA-Binding ProteinsIon Channel GatingLymphocyte ActivationMembrane PotentialsMiceMice, Inbred C3HMice, Inbred C57BLMutationNFATC Transcription FactorsNuclear ProteinsPatch-Clamp TechniquesPhosphorylationProtein SubunitsReceptors, Antigen, T-CellT-LymphocytesTranscription FactorsConceptsT lymphocytesCalcium channelsVoltage-gated calcium channelsT lymphocyte functionT cell receptor stimulationCell receptor stimulationCytokine productionLymphocyte functionCalcium influxReceptor stimulationCalcium responseCalcium entryTranscription factor NFATCav1 channelsLymphocytesAlpha1 subunitCav channelsNormal functionNonexcitable cellsDisplay impairmentsExcitable cellsChannel openingMolecular identityDiverse physiological processesPhysiological processes
2000
Regulation of volume‐activated chloride channels by P‐glycoprotein: phosphorylation has the final say!
Idriss H, Hannun Y, Boulpaep E, Basavappa S. Regulation of volume‐activated chloride channels by P‐glycoprotein: phosphorylation has the final say! The Journal Of Physiology 2000, 524: 629-636. PMID: 10790147, PMCID: PMC2269906, DOI: 10.1111/j.1469-7793.2000.00629.x.Peer-Reviewed Original ResearchConceptsProtein kinase CReversible phosphorylationChloride channelsChloride channel activityPhosphorylation of PgpSuch phosphorylationMultiple phosphorylationVolume-activated chloride channelsTransmembrane transportersKinase CPhosphorylationInhibition of transportCell volume changesPossible regulationChannel activityP-glycoproteinPotential involvementSuch regulationRegulation functionRegulationUnrelated drugsPgpProteinTransportersOverexpression
1998
Properties of an Inwardly Rectifying ATP-sensitive K+ Channel in the Basolateral Membrane of Renal Proximal Tubule
Mauerer U, Boulpaep E, Segal A. Properties of an Inwardly Rectifying ATP-sensitive K+ Channel in the Basolateral Membrane of Renal Proximal Tubule. The Journal Of General Physiology 1998, 111: 139-160. PMID: 9417141, PMCID: PMC1887768, DOI: 10.1085/jgp.111.1.139.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine TriphosphateAmbystomaAnimalsBariumBiological TransportCationsCells, CulturedCytidine TriphosphateDiazoxideDiureticsElectric ConductivityGlyburideGuanosine TriphosphateHypoglycemic AgentsInosine TriphosphateIon Channel GatingKidney Tubules, ProximalKineticsMicrovilliPatch-Clamp TechniquesPotassium ChannelsSodium Chloride Symporter InhibitorsSodium-Potassium-Exchanging ATPaseThalliumThymine NucleotidesUridine TriphosphateConceptsProximal tubule cellsProximal tubulesTubule cellsBasolateral membraneChannel opener diazoxideChannel activityPump-leak couplingRenal proximal tubulesPivotal physiological rolesOpener diazoxideMillimolar dosesMM ATPHigh dosesPotassium conductanceCell membrane potentialInternal Mg2Cytosolic additionATPase pumpRegulation of an Inwardly Rectifying ATP-sensitive K+ Channel in the Basolateral Membrane of Renal Proximal Tubule
Mauerer U, Boulpaep E, Segal A. Regulation of an Inwardly Rectifying ATP-sensitive K+ Channel in the Basolateral Membrane of Renal Proximal Tubule. The Journal Of General Physiology 1998, 111: 161-180. PMID: 9417142, PMCID: PMC1887764, DOI: 10.1085/jgp.111.1.161.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine TriphosphateAmbystomaAnimalsBiological TransportCalciumCell MembraneColforsinCyclic AMP-Dependent Protein KinasesEnzyme ActivationEpithelial CellsHydrogen-Ion ConcentrationIon Channel GatingKidney Tubules, ProximalPatch-Clamp TechniquesPhosphorylationPotassium ChannelsProtein Kinase CSodium-Potassium-Exchanging ATPaseConceptsBasolateral membraneProtein kinase AActin cytoskeletonATPase pumpOuter membraneProtein kinaseKinase ACellular metabolismKATP channelsSecond messengerStimulation of transportTransport activityPhysiological importanceMembrane stretchPhorbol esterChannel activityMembrane patchesRegulationIntracellularO patchesFunctional couplingHypotonic swellingCell-attached patchesCell depolarizationRenal proximal tubules
1995
Primary structure and functional expression of a cGMP-gated potassium channel.
Yao X, Segal AS, Welling P, Zhang X, McNicholas CM, Engel D, Boulpaep EL, Desir GV. Primary structure and functional expression of a cGMP-gated potassium channel. Proceedings Of The National Academy Of Sciences Of The United States Of America 1995, 92: 11711-11715. PMID: 8524834, PMCID: PMC40472, DOI: 10.1073/pnas.92.25.11711.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBase SequenceCloning, MolecularCyclic GMPElectric ConductivityGene LibraryIon Channel GatingMolecular Sequence DataOocytesPhylogenyPotassiumPotassium ChannelsProtein BiosynthesisProtein ConformationRabbitsRNA, MessengerSequence Homology, Amino AcidTissue DistributionXenopusConceptsDeduced amino acid sequenceChannel protein phosphorylationCysteine-rich regionAmino acid sequenceNorthern blot analysisPotassium channel activityProtein phosphorylationAcid sequenceGene expressionPrimary structureFunctional expressionK channelsIon channelsChannel activityBlot analysisCyclic nucleotidesShaker K channelsPotassium channelsEffects of substancesKCN1Intracellular cGMPCGMPNitric oxideExpressionImportant role
1992
Mouse cortical collecting duct cells show nonselective cation channel activity and express a gene related to the cGMP-gated rod photoreceptor channel.
Ahmad I, Korbmacher C, Segal A, Cheung P, Boulpaep E, Barnstable C. Mouse cortical collecting duct cells show nonselective cation channel activity and express a gene related to the cGMP-gated rod photoreceptor channel. Proceedings Of The National Academy Of Sciences Of The United States Of America 1992, 89: 10262-10266. PMID: 1279673, PMCID: PMC50318, DOI: 10.1073/pnas.89.21.10262.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBase SequenceBlotting, NorthernCell LineCyclic GMPDNAIon Channel GatingIon ChannelsKidney CortexKidney Tubules, CollectingMembrane PotentialsMiceMolecular Sequence DataOligodeoxyribonucleotidesPhotoreceptor CellsPoly APolymerase Chain ReactionRatsRNARNA, MessengerSequence Homology, Nucleic AcidConceptsNonselective cation channelsPhotoreceptor channelDuct cellsCation channel probeCation channelsChannel activityPolymerase chain reactionNonselective cation channel activityCGMP decreaseCation channel activityChannel subunitsCytoplasmic applicationChain reactionRod photoreceptorsNorthern blot analysisRetinal cGMPBlot analysisCGMPRat kidney cDNA libraryChannel genesMiceSingle-channel conductanceOpen probabilityCellsCalcium removal