1999
Gramicidin channel controversy — the structure in a lipid environment
Andersen O, Apell H, Bamberg E, Busath D, Koeppe R, Sigworth F, Szabo G, Urry D, Woolley A. Gramicidin channel controversy — the structure in a lipid environment. Nature Structural & Molecular Biology 1999, 6: 609-609. PMID: 10404209, DOI: 10.1038/10648.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 transitionResiduesFunctional 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
1992
Tandem linkage of Shaker K+ channel subunits does not ensure the stoichiometry of expressed channels
McCormack K, Lin L, Iverson L, Tanouye M, Sigworth F. Tandem linkage of Shaker K+ channel subunits does not ensure the stoichiometry of expressed channels. Biophysical Journal 1992, 63: 1406-1411. PMID: 1477286, PMCID: PMC1261445, DOI: 10.1016/s0006-3495(92)81703-4.Peer-Reviewed Original Research
1989
Primary structure and functional expression of a mammalian skeletal muscle sodium channel
Trimmer J, Cooperman S, Tomiko S, Zhou J, Crean S, Boyle M, Kalen R, Sheng Z, Barchi R, Sigworth F, Goodman R, Agnew W, Mandel G. Primary structure and functional expression of a mammalian skeletal muscle sodium channel. Neuron 1989, 3: 33-49. PMID: 2559760, DOI: 10.1016/0896-6273(89)90113-x.Peer-Reviewed Original ResearchConceptsAlpha subunitHomologous domains IAmino acid segmentSodium channelsSkeletal muscle sodium channelsNorthern blot analysisSkeletal muscleMuscle sodium channelsVoltage-sensitive sodium channelsPrimary structureFunctional expressionDomain IAcid segmentNative channelsSynthetic RNAXenopus oocytesRat muscle fibersBlot analysisRat skeletal muscleEel electroplaxRat brainSubunitsMuscle fibersMuscleCDNATransmembrane Channels Based on Tartaric Acid-Gramicidin A Hybrids
Stankovic C, Heinemann S, Delfino J, Sigworth F, Schreiber S. Transmembrane Channels Based on Tartaric Acid-Gramicidin A Hybrids. Science 1989, 244: 813-817. PMID: 2471263, DOI: 10.1126/science.2471263.Peer-Reviewed Original Research