2009
Structure of the BK potassium channel in a lipid membrane from electron cryomicroscopy
Wang L, Sigworth FJ. Structure of the BK potassium channel in a lipid membrane from electron cryomicroscopy. Nature 2009, 461: 292-295. PMID: 19718020, PMCID: PMC2797367, DOI: 10.1038/nature08291.Peer-Reviewed Original ResearchConceptsVoltage sensor domainNative membrane environmentMembrane proteinsMembrane environmentChannel voltage-sensor domainElectron cryomicroscopyVoltage-activated potassium channelsSingle-particle electron cryomicroscopyIndividual protein particlesPotassium channelsBK potassium channelsLarge conductance calciumLipid membranesX-ray crystal structureBK channelsStructural studiesProtein particlesProteinCryomicroscopyCrystal structureFormation of crystalsDomainStructureCrystalsChannels
1996
Impaired slow inactivation in mutant sodium channels
Cummins T, Sigworth F. Impaired slow inactivation in mutant sodium channels. Biophysical Journal 1996, 71: 227-236. PMID: 8804606, PMCID: PMC1233474, DOI: 10.1016/s0006-3495(96)79219-6.Peer-Reviewed Original ResearchConceptsRat skeletal muscle channelsSodium currentProlonged depolarizationSlow inactivationPersistent sodium currentMaximal sodium currentSkeletal muscle channelsMuscle paralysisSkeletal muscle fibersMutant sodium channelsSustained currentHyperkalemic periodic paralysisM mutationPeriodic paralysisSodium channelsMuscle channelsMuscle fibersParalysisFast inactivationWild-type channelsMutant channelsDepolarization
1993
Functional expression and purification of a homomeric human alpha 1 glycine receptor in baculovirus-infected insect cells.
Cascio M, Schoppa N, Grodzicki R, Sigworth F, Fox R. Functional expression and purification of a homomeric human alpha 1 glycine receptor in baculovirus-infected insect cells. Journal Of Biological Chemistry 1993, 268: 22135-22142. PMID: 8408073, DOI: 10.1016/s0021-9258(20)80658-9.Peer-Reviewed Original ResearchConceptsInsect cellsGlyR proteinSf9 cellsMembrane protein channelsSf9 insect cellsSodium dodecyl sulfate-polyacrylamide gelsDodecyl sulfate-polyacrylamide gelsSulfate-polyacrylamide gelsWhole cell lysatesHuman kidney cell lineShares sequenceKidney cell lineTransient expressionExpression systemStructural homologyChannel proteinsBiophysical characterizationProtein channelsFunctional channelsFunctional expressionMembrane fractionNative channelsCell surfaceGlycine receptorsChloride channels
1991
Changes in channel properties of acetylcholine receptors during the time course of thiol chemical modifications
Bouzat C, Barrantes F, Sigworth F. Changes in channel properties of acetylcholine receptors during the time course of thiol chemical modifications. Pflügers Archiv - European Journal Of Physiology 1991, 418: 51-61. PMID: 2041725, DOI: 10.1007/bf00370451.Peer-Reviewed Original ResearchConceptsSingle acetylcholine receptor channelsHigh agonist concentrationsPatch-clamp techniqueOpen timeConcentration of NEMSilent periodAcetylcholine receptorsN-ethylmaleimideAcetylcholine receptor channelsAgonist concentrationsChannel open probabilityReceptor channelsAChRMM N-ethylmaleimideTime of exposureRate of occurrenceSingle-channel currentsTime courseNEM treatmentControl receptorsReceptorsSignificant changesTreatmentShort openingsSlight reduction
1990
Activation of Torpedo acetylcholine receptors expressed in mouse fibroblasts. Single channel current kinetics reveal distinct agonist binding affinities.
Sine S, Claudio T, Sigworth F. Activation of Torpedo acetylcholine receptors expressed in mouse fibroblasts. Single channel current kinetics reveal distinct agonist binding affinities. The Journal Of General Physiology 1990, 96: 395-437. PMID: 1698917, PMCID: PMC2228994, DOI: 10.1085/jgp.96.2.395.Peer-Reviewed Original Research
1987
Genetic Reconstitution of Functional Acetylcholine Receptor Channels in Mouse Fibroblasts
Claudio T, Green W, Hartman D, Hayden D, Paulson H, Sigworth F, Sine S, Swedlund A. Genetic Reconstitution of Functional Acetylcholine Receptor Channels in Mouse Fibroblasts. Science 1987, 238: 1688-1694. PMID: 3686008, DOI: 10.1126/science.3686008.Peer-Reviewed Original ResearchConceptsExpression systemDNA-mediated gene transfer techniquesMouse fibroblast cellsDNA-mediated gene transferLigand-gated ion channelsCell surface AChRsNew expression systemFibroblast cellsTorpedo AChRClonal cell linesGene transfer techniquesForeign genesGene productsGenetic reconstitutionRecombinant DNACellular componentsTorpedo acetylcholine receptorComplementary DNASurface AChRsAcetylcholine receptor channelsFunctional consequencesGene transferIon channelsHomogenous cellsMouse fibroblasts