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 ResearchMeSH KeywordsAnimalsBase SequenceBinding SitesIon Channel GatingKidneyMolecular Sequence DataMutationPatch-Clamp TechniquesPotassium ChannelsRabbitsShaker Superfamily of Potassium ChannelsStructure-Activity RelationshipConceptsN-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
1998
Characterization of a Regulatory Region in the N-Terminus of Rabbit Kv1.3
Yao X, Huang Y, Kwan HY, Chan P, Segal AS, Desir G. Characterization of a Regulatory Region in the N-Terminus of Rabbit Kv1.3. Biochemical And Biophysical Research Communications 1998, 249: 492-498. PMID: 9712724, DOI: 10.1006/bbrc.1998.9122.Peer-Reviewed Original ResearchAmino Acid SequenceAnimalsChemical PhenomenaChemistry, PhysicalDynaminsElectric ConductivityEndocytosisFemaleGene DeletionGene ExpressionGTP PhosphohydrolasesKv1.3 Potassium ChannelMolecular Sequence DataMutagenesisOocytesPeptide FragmentsPotassium ChannelsPotassium Channels, Voltage-GatedProtein Sorting SignalsRabbitsRNA, ComplementaryStructure-Activity RelationshipTransfectionXenopus laevis