2002
Regulation of the voltage-gated K+ channel KCNA10 by KCNA4B, a novel β-subunit
Tian S, Liu W, Wu Y, Rafi H, Segal AS, Desir GV. Regulation of the voltage-gated K+ channel KCNA10 by KCNA4B, a novel β-subunit. American Journal Of Physiology. Renal Physiology 2002, 283: f142-f149. PMID: 12060596, DOI: 10.1152/ajprenal.00258.2001.Peer-Reviewed Original Research
2000
KCNA10: a novel ion channel functionally related to both voltage-gated potassium and CNG cation channels
Lang R, Lee G, Liu W, Tian S, Rafi H, Orias M, Segal A, Desir G. KCNA10: a novel ion channel functionally related to both voltage-gated potassium and CNG cation channels. American Journal Of Physiology. Renal Physiology 2000, 278: f1013-f1021. PMID: 10836990, DOI: 10.1152/ajprenal.2000.278.6.f1013.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBase SequenceCyclic Nucleotide-Gated Cation ChannelsDNA PrimersFemaleHumansIn Vitro TechniquesIon Channel GatingIon ChannelsMembrane PotentialsOocytesPatch-Clamp TechniquesPotassium Channel BlockersPotassium ChannelsPotassium Channels, Voltage-GatedRabbitsRecombinant ProteinsSecond Messenger SystemsShaker Superfamily of Potassium ChannelsXenopus laevis
1999
The T0 Domain of Rabbit KV1.3 Regulates Steady State Channel Protein Level
Segal A, Yao X, Desir G. The T0 Domain of Rabbit KV1.3 Regulates Steady State Channel Protein Level. Biochemical And Biophysical Research Communications 1999, 254: 54-64. PMID: 9920732, DOI: 10.1006/bbrc.1998.9801.Peer-Reviewed Original ResearchConceptsN-terminal regulatory regionVoltage-gated potassium channelsWild-type channelsRegulatory regionsPlasma membraneAmino terminusChannel assemblyChannel proteinsRecognition domainSingle-channel conductanceKv channelsChannel protein levelsProtein levelsProtein densityPotassium channelsOpen probabilityType channelsChannel conductanceKv1.3Fast inactivationDomainMembraneTerminusProteinInactivation
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 roleMolecular characterization of voltage and cyclic nucleotide-gated potassium channels in kidney
Desir G. Molecular characterization of voltage and cyclic nucleotide-gated potassium channels in kidney. Kidney International 1995, 48: 1031-1035. PMID: 8569064, DOI: 10.1038/ki.1995.386.Peer-Reviewed Original ResearchConceptsRenal K channelsMolecular characterizationInitial molecular characterizationPotassium channelsMammalian cellsMembrane proteinsMolecular biologyCell membraneK channelsDiverse groupPhysiologic roleKinetic propertiesPotential physiologic rolePassive movementBiologyProteinPhysiologyKidneyMembraneCharacterizationCellsExtensive dataThe structure, regulation and pathophysiology of potassium channels
Desir G. The structure, regulation and pathophysiology of potassium channels. Current Opinion In Nephrology & Hypertension 1995, 4: 402-405. PMID: 8564442, DOI: 10.1097/00041552-199509000-00005.Peer-Reviewed Original Research
1992
Molecular physiology of renal potassium channels.
Desir G. Molecular physiology of renal potassium channels. Seminars In Nephrology 1992, 12: 531-40. PMID: 1475548.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsHumansHypertensionIon Channel GatingKidneyMembrane PotentialsMolecular BiologyPotassium ChannelsConceptsRenal potassium channelsExtensive physiological dataMolecular biological techniquesMolecular physiologyImportant disease statesEnormous diversityK channelsIon channelsMolecular informationCellular proliferationBiological techniquesPotassium channelsRecent appreciationPossible roleDisease statesK transportMajor rolePatch-clamp techniqueDiversityPhysiological dataChannel structurePhysiologyRegulationRoleProliferationIsolation of putative voltage-gated epithelial K-channel isoforms from rabbit kidney and LLC-PK1 cells
Desir GV, Hamlin HA, Puente E, Reilly RF, Hildebrandt F, Igarashi P. Isolation of putative voltage-gated epithelial K-channel isoforms from rabbit kidney and LLC-PK1 cells. American Journal Of Physiology 1992, 262: f151-f157. PMID: 1733291, DOI: 10.1152/ajprenal.1992.262.1.f151.Peer-Reviewed Original ResearchConceptsDeduced amino acid sequenceAmino acid sequenceAcid sequenceVoltage-gated K channelsRabbit genomic DNAPutative transmembrane segmentsShaker-like genesPutative voltage sensorShaker gene familyVoltage-gated potassium channelsGene familyShaker proteinRenal epithelial cellsTransmembrane segmentsSequence similarityRabbit cDNAEpithelial cell lineSouthern analysisProtein sequencesLLC-PK1 cellsDifferent genesGenomic DNAKidney cDNACDNAS4 segment