2007
Four-turn α-Helical Segment Prevents Surface Expression of the Auxiliary hβ2 Subunit of BK-type Channel*
Lv C, Chen M, Gan G, Wang L, Xu T, Ding J. Four-turn α-Helical Segment Prevents Surface Expression of the Auxiliary hβ2 Subunit of BK-type Channel*. Journal Of Biological Chemistry 2007, 283: 2709-2715. PMID: 17991741, DOI: 10.1074/jbc.m704440200.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsCell LineEndoplasmic ReticulumGene ExpressionHumansLarge-Conductance Calcium-Activated Potassium ChannelsMicroscopy, FluorescenceModels, MolecularMolecular Sequence DataMutagenesis, Site-DirectedPatch-Clamp TechniquesProtein Structure, SecondaryProtein SubunitsRatsRecombinant Fusion ProteinsSequence Homology, Amino AcidConceptsBK-type channelsSurface expressionRat chromaffin cellsExtracellular loopPancreatic beta cellsTrafficking mechanismsN-terminusDRG neuronsHelical segmentsToxin sensitivityBeta cellsClamp techniqueHelp of immunofluorescenceAuxiliary beta subunitsAlpha-helical segmentsChromaffin cellsBeta2 subunitBK channelsHbeta2Retention signalChannel regulatorRegulatory mechanismsBeta subunitEndoplasmic reticulumLarge conductance
2006
Residue Phe266 in S5-S6 loop is not critical for Charybdotoxin binding to Ca2+-activated K+ (mSlo1) channels
Yao J, Li H, Gan G, Wu Y, Ding J. Residue Phe266 in S5-S6 loop is not critical for Charybdotoxin binding to Ca2+-activated K+ (mSlo1) channels. Acta Pharmacologica Sinica 2006, 27: 945-949. PMID: 16787581, DOI: 10.1111/j.1745-7254.2006.00385.x.Peer-Reviewed Original Research