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
1998
Activation of Shaker Potassium Channels
Schoppa N, Sigworth F. Activation of Shaker Potassium Channels. The Journal Of General Physiology 1998, 111: 295-311. PMID: 9450945, PMCID: PMC2222768, DOI: 10.1085/jgp.111.2.295.Peer-Reviewed Original ResearchActivation of Shaker Potassium Channels
Schoppa N, Sigworth F. Activation of Shaker Potassium Channels. The Journal Of General Physiology 1998, 111: 313-342. PMID: 9450946, PMCID: PMC2222769, DOI: 10.1085/jgp.111.2.313.Peer-Reviewed Original ResearchActivation of Shaker Potassium Channels
Schoppa N, Sigworth F. Activation of Shaker Potassium Channels. The Journal Of General Physiology 1998, 111: 271-294. PMID: 9450944, PMCID: PMC2222764, DOI: 10.1085/jgp.111.2.271.Peer-Reviewed Original Research
1997
Enhanced Closed-state Inactivation in a Mutant Shaker K+ Channel
Ayer, Jr. R, Sigworth F. Enhanced Closed-state Inactivation in a Mutant Shaker K+ Channel. The Journal Of Membrane Biology 1997, 157: 215-230. PMID: 9178609, DOI: 10.1007/s002329900230.Peer-Reviewed Original Research
1994
Voltage gating of ion channels
Sigworth F. Voltage gating of ion channels. Quarterly Reviews Of Biophysics 1994, 27: 1-40. PMID: 7520590, DOI: 10.1017/s0033583500002894.Peer-Reviewed Original ResearchConceptsVoltage-gated calcium channelsNerve action potentialsVoltage-gated sodium channelsRelease of hormonesIon channelsVoltage-gated ion channelsCalcium channelsAction potentialsNeurotransmitter releaseMuscle contractionSodium channelsMembrane proteinsCellular signalsVoltage gatingCentral roleHormoneRelease
1993
Substitution of a hydrophobic residue alters the conformational stability of Shaker K+ channels during gating and assembly
McCormack K, Lin L, Sigworth F. Substitution of a hydrophobic residue alters the conformational stability of Shaker K+ channels during gating and assembly. Biophysical Journal 1993, 65: 1740-1748. PMID: 8274662, PMCID: PMC1225901, DOI: 10.1016/s0006-3495(93)81202-5.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBase SequenceBiophysical PhenomenaBiophysicsDNA, ComplementaryDrosophilaDrug StabilityFemaleIon Channel GatingMembrane PotentialsMolecular Sequence DataMutagenesis, Site-DirectedOocytesPeptidesPotassium ChannelsProtein ConformationShaker Superfamily of Potassium ChannelsThermodynamicsXenopus laevisConceptsUncharged amino acid residuesLeucine heptad repeatWild-type subunitsPosition 370Large hydrophobic residuesAmino acid residuesSequence motifsConservative substitutionsHeptad repeatHydrophobic residuesVoltage-gated channelsLeucine residuesAcid residuesTertiary structureS4 segmentSpecific hydrophobic interactionsHydrophilic residuesResidue altersChannel subunitsInactivation gatingChannel complexSubunitsConformational stabilityConformational transitionResiduesFluctuations in ion channel gating currents. Analysis of nonstationary shot noise
Crouzy S, Sigworth F. Fluctuations in ion channel gating currents. Analysis of nonstationary shot noise. Biophysical Journal 1993, 64: 68-76. PMID: 8381683, PMCID: PMC1262303, DOI: 10.1016/s0006-3495(93)81341-9.Peer-Reviewed Original Research
1992
[52] Analysis of nonstationary single-channel currents
Sigworth F, Zhou J. [52] Analysis of nonstationary single-channel currents. Methods In Enzymology 1992, 207: 746-762. PMID: 1382211, DOI: 10.1016/0076-6879(92)07054-r.Peer-Reviewed Original Research