Shumin Bian
Safety Advisor – Team LeadCards
About
Research
Publications
2025
CryoEM structures of Kv1.2 potassium channels, conducting and non-conducting
Wu Y, Yan Y, Yang Y, Bian S, Rivetta A, Allen K, Sigworth F. CryoEM structures of Kv1.2 potassium channels, conducting and non-conducting. ELife 2025, 12: rp89459. PMID: 39945513, PMCID: PMC11825129, DOI: 10.7554/elife.89459.Peer-Reviewed Original ResearchConceptsIon occupancyIon binding sitesTerminal amineSelectivity filterIon densityLow-resolution structureProtein conformationIonsDetergent micellesPotassium channelsToxin blockVoltage-gated potassium channel Kv1.2Non-conductingStructureVoltage-gated potassium channelsPotassium channel Kv1.2Kv1.2 potassium channelChannel's outer mouthBinding sitesAminesCarbonylCryoEM structures of Kv1.2 potassium channels, conducting and non-conducting
Wu Y, Yan Y, Yang Y, Bian S, Rivetta A, Allen K, Sigworth F. CryoEM structures of Kv1.2 potassium channels, conducting and non-conducting. ELife 2025, 12 DOI: 10.7554/elife.89459.4.Peer-Reviewed Original ResearchIon occupancyIon binding sitesTerminal amineIon densitySelectivity filterLow-resolution structureProtein conformationIonsDetergent micellesPotassium channelsToxin blockVoltage-gated potassium channel Kv1.2Non-conductingStructureVoltage-gated potassium channelsPotassium channel Kv1.2Kv1.2 potassium channelChannel's outer mouthBinding sites
2017
Current carried by the Slc26 family member prestin does not flow through the transporter pathway
Bai JP, Moeini-Naghani I, Zhong S, Li FY, Bian S, Sigworth FJ, Santos-Sacchi J, Navaratnam D. Current carried by the Slc26 family member prestin does not flow through the transporter pathway. Scientific Reports 2017, 7: 46619. PMID: 28422190, PMCID: PMC5395958, DOI: 10.1038/srep46619.Peer-Reviewed Original Research
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 ionsChloride Flux in Prestin-Expressing Cells
Zhong S, Bian S, Navaratnam D, Santos-Sacchi J. Chloride Flux in Prestin-Expressing Cells. Biophysical Journal 2012, 102: 246a. DOI: 10.1016/j.bpj.2011.11.1355.Peer-Reviewed Original Research
2011
Interactions between β-Catenin and the HSlo Potassium Channel Regulates HSlo Surface Expression
Bian S, Bai JP, Chapin H, Le Moellic C, Dong H, Caplan M, Sigworth FJ, Navaratnam DS. Interactions between β-Catenin and the HSlo Potassium Channel Regulates HSlo Surface Expression. PLOS ONE 2011, 6: e28264. PMID: 22194818, PMCID: PMC3237428, DOI: 10.1371/journal.pone.0028264.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsbeta CateninBinding SitesBiological AssayCell MembraneChickensGene Knockdown TechniquesHair Cells, AuditoryHEK293 CellsHumansImmunoprecipitationIntercellular JunctionsKineticsLarge-Conductance Calcium-Activated Potassium Channel alpha SubunitsModels, MolecularMolecular Sequence DataMutant ProteinsMutationPhosphorylationProtein BindingProtein TransportRNA, Small InterferingSequence DeletionTransfectionWnt Signaling PathwayConceptsΒ-cateninS10 regionHEK cellsSurface expressionCell biology toolsPotassium channel alpha subunitΒ-catenin interactionDownregulation of WntCytoskeleton frameworkChannel alpha subunitChicken hair cellsPhosphorylation sitesDeletion mutantsBiology toolsΒ-catenin-dependent canonical WntAlpha subunitCanonical WntMultiple binding sitesNumber of diseasesStable bindingWntPhysiological significanceBinding sitesReduced expressionHair cellsEvaluating Prestin's Changing Biophysical Attributes in Development Using a Tet‐Induced Cell Line
Bian S, Koo B, Kelleher S, Santos-Sacchi J, Navaratnam D, Shera C, Olson E. Evaluating Prestin's Changing Biophysical Attributes in Development Using a Tet‐Induced Cell Line. AIP Conference Proceedings 2011, 1403: 143-147. DOI: 10.1063/1.3658075.Peer-Reviewed Original ResearchExtracellular chloride regulation of Kv2.1, contributor to the major outward Kv current in mammalian outer hair cells
Li X, Surguchev A, Bian S, Navaratnam D, Santos-Sacchi J. Extracellular chloride regulation of Kv2.1, contributor to the major outward Kv current in mammalian outer hair cells. American Journal Of Physiology - Cell Physiology 2011, 302: c296-c306. PMID: 21940671, PMCID: PMC4054960, DOI: 10.1152/ajpcell.00177.2011.Peer-Reviewed Original Research
2010
A highly expressing Tet-inducible cell line recapitulates in situ developmental changes in prestin's Boltzmann characteristics and reveals early maturational events
Bian S, Koo BW, Kelleher S, Santos-Sacchi J, Navaratnam DS. A highly expressing Tet-inducible cell line recapitulates in situ developmental changes in prestin's Boltzmann characteristics and reveals early maturational events. American Journal Of Physiology - Cell Physiology 2010, 299: c828-c835. PMID: 20631244, PMCID: PMC3774197, DOI: 10.1152/ajpcell.00182.2010.Peer-Reviewed Original Research
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