2013
Real Time Measures of Prestin Charge and Fluorescence during Plasma Membrane Trafficking Reveal Sub-Tetrameric Activity
Bian S, Navaratnam D, Santos-Sacchi J. Real Time Measures of Prestin Charge and Fluorescence during Plasma Membrane Trafficking Reveal Sub-Tetrameric Activity. PLOS ONE 2013, 8: e66078. PMID: 23762468, PMCID: PMC3677934, DOI: 10.1371/journal.pone.0066078.Peer-Reviewed Original ResearchConceptsObligate tetramerPlasma membraneMembrane motor proteinIntegral membrane proteinsTetracycline-inducible cell lineMembrane proteinsMotor proteinsPrestin densityTemperature blockPrestinFluorescence measuresMembrane fluorescenceCell linesNonlinear capacitanceCochlear amplificationProteinTetramerMembraneFluorescencePrevious observationsVoltage clampFluorescence methodCellsAmplification
2012
Expression, Purification and Functional Reconstitution of Slack Sodium-Activated Potassium Channels
Yan Y, Yang Y, Bian S, Sigworth FJ. Expression, Purification and Functional Reconstitution of Slack Sodium-Activated Potassium Channels. The Journal Of Membrane Biology 2012, 245: 667-674. PMID: 22729647, PMCID: PMC3903048, DOI: 10.1007/s00232-012-9425-7.Peer-Reviewed Original ResearchConceptsPotassium channel activityΑ-subunitPotassium channel α-subunitChannel activityGene codesFunctional reconstitutionMembrane vesiclesChannel familyCell typesPlanar bilayer membranesPotassium channelsBilayer membranesExpressionReconstitutionPurificationProteinVesiclesMembraneActivityFamilySodium ions
2010
Combinatorial Cysteine Mutagenesis Reveals a Critical Intramonomer Role for Cysteines in Prestin Voltage Sensing
Bai JP, Surguchev A, Bian S, Song L, Santos-Sacchi J, Navaratnam D. Combinatorial Cysteine Mutagenesis Reveals a Critical Intramonomer Role for Cysteines in Prestin Voltage Sensing. Biophysical Journal 2010, 99: 85-94. PMID: 20655836, PMCID: PMC2895379, DOI: 10.1016/j.bpj.2010.03.066.Peer-Reviewed Original ResearchConceptsDisulfide bond formationCysteine residuesCysteine residue pairsSingle cysteine residueCysteine mutagenesisTransmembrane proteinSubstitution mutantsSLC26 familyResidue pairsFörster resonance energy transferCharge movementVoltage-dependent charge movementDisulfide interactionsResonance energy transferPrestinProteinMutantsDimer formationResiduesCysteineHair cellsSurface expressionAnion transportersCochlear amplificationWestern blot
2001
Ca2+-binding activity of a COOH-terminal fragment of the Drosophila BK channel involved in Ca2+-dependent activation
Bian S, Favre I, Moczydlowski E. Ca2+-binding activity of a COOH-terminal fragment of the Drosophila BK channel involved in Ca2+-dependent activation. Proceedings Of The National Academy Of Sciences Of The United States Of America 2001, 98: 4776-4781. PMID: 11274367, PMCID: PMC31910, DOI: 10.1073/pnas.081072398.Peer-Reviewed Original ResearchConceptsIntracellular COOH-terminal domainDependent activationBK channelsCOOH-terminal domainProtein blot assayBiochemical approachesStructural basisBiophysical analysisBK proteinAsp residuesControl proteinHEK293 cellsEscherichia coliProteinElectrophysiological assaysBlot assaysLarge conductanceTerminal fragmentSoluble formActivationResiduesFunctional correlationSpecific bindingSpecific regionsBinding