2000
Identification of the Cystic Fibrosis Transmembrane Conductance Regulator Domains That Are Important for Interactions with ROMK2*
Cahill P, Nason M, Ambrose C, Yao T, Thomas P, Egan M. Identification of the Cystic Fibrosis Transmembrane Conductance Regulator Domains That Are Important for Interactions with ROMK2*. Journal Of Biological Chemistry 2000, 275: 16697-16701. PMID: 10748197, DOI: 10.1074/jbc.m910205199.Peer-Reviewed Original ResearchConceptsCystic fibrosis transmembrane conductance regulatorR domainCAMP-activated chloride channelFunctional chloride channelChloride channelsFibrosis transmembrane conductance regulatorFirst transmembrane domainTransmembrane domain 2Transmembrane domain 1Transmembrane conductance regulatorRegulator domainFold domainCFTR domainsTransmembrane domainCFTR regulationCFTR constructsConductance regulatorFirst nucleotideDomain 2Regulatory propertiesDomain 1Ion channelsXenopus oocytesPhosphorylationGlibenclamide sensitivity
1996
Sensitivity of a renal K+ channel (ROMK2) to the inhibitory sulfonylurea compound glibenclamide is enhanced by coexpression with the ATP-binding cassette transporter cystic fibrosis transmembrane regulator.
McNicholas C, Guggino W, Schwiebert E, Hebert S, Giebisch G, Egan M. Sensitivity of a renal K+ channel (ROMK2) to the inhibitory sulfonylurea compound glibenclamide is enhanced by coexpression with the ATP-binding cassette transporter cystic fibrosis transmembrane regulator. Proceedings Of The National Academy Of Sciences Of The United States Of America 1996, 93: 8083-8088. PMID: 8755607, PMCID: PMC38879, DOI: 10.1073/pnas.93.15.8083.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine TriphosphateAnimalsChloride ChannelsCyclic AMP-Dependent Protein KinasesCystic Fibrosis Transmembrane Conductance RegulatorFemaleGlyburideKidneyMembrane PotentialsOocytesPatch-Clamp TechniquesPhosphorylationPotassium ChannelsPotassium Channels, Inwardly RectifyingSodium ChannelsXenopus laevis