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 channelsFunctional consequences of a Na+ channel mutation causing hyperkalemic periodic paralysis
Cummins T, Zhou J, Sigworth F, Ukomadu C, Stephan M, Ptáčk L, Agnew W. Functional consequences of a Na+ channel mutation causing hyperkalemic periodic paralysis. Neuron 1993, 10: 667-678. PMID: 8386527, DOI: 10.1016/0896-6273(93)90168-q.Peer-Reviewed Original ResearchConceptsHyperkalemic periodic paralysisFifth transmembrane segmentHuman embryonic kidney 293 cellsSingle base pair substitutionsEmbryonic kidney 293 cellsKidney 293 cellsBase pair substitutionsTransmembrane segmentsHuman mutationsChannel cDNARat channelHuman skeletal muscleFunctional consequencesPair substitutionsSecond domainCorresponding regionChannel mutationsGenetic defectsMutationsSkeletal musclePeriodic paralysisPatch-clamp recordingsCDNARat musclePedigree