2014
Clinical whole-genome sequencing in severe early-onset epilepsy reveals new genes and improves molecular diagnosis
Martin HC, Kim GE, Pagnamenta AT, Murakami Y, Carvill GL, Meyer E, Copley RR, Rimmer A, Barcia G, Fleming MR, Kronengold J, Brown MR, Hudspith KA, Broxholme J, Kanapin A, Cazier JB, Kinoshita T, Nabbout R, Consortium T, Bentley D, McVean G, Heavin S, Zaiwalla Z, McShane T, Mefford HC, Shears D, Stewart H, Kurian MA, Scheffer IE, Blair E, Donnelly P, Kaczmarek LK, Taylor JC. Clinical whole-genome sequencing in severe early-onset epilepsy reveals new genes and improves molecular diagnosis. Human Molecular Genetics 2014, 23: 3200-3211. PMID: 24463883, PMCID: PMC4030775, DOI: 10.1093/hmg/ddu030.Peer-Reviewed Original ResearchMeSH KeywordsChildChild, PreschoolChromosomes, Human, Pair 9EpilepsyGenetic Predisposition to DiseaseGenome-Wide Association StudyHigh-Throughput Nucleotide SequencingHumansKCNQ2 Potassium ChannelMaleMembrane ProteinsMutationNAV1.2 Voltage-Gated Sodium ChannelNerve Tissue ProteinsPathology, MolecularPotassium ChannelsPotassium Channels, Sodium-ActivatedProto-Oncogene Proteins c-cblUniparental DisomyYoung AdultConceptsSevere early-onset epilepsyEarly-onset epilepsyOhtahara syndromeMolecular diagnosisWhole-genome sequencingClinical whole-genome sequencingPathogenic de novo mutationsHomozygous missense variantPotassium channel currentsSeizure typesO patientsDiagnostic yieldOS casesPatientsPower of WGSMolecular genetic diagnosisEpilepsyClinical phenotypeClinical diagnosisClinical toolHeterogeneous disorderDevelopmental delayDe novo mutationsDiagnosisMissense variants
2003
BAK Alters Neuronal Excitability and Can Switch from Anti- to Pro-Death Function during Postnatal Development
Fannjiang Y, Kim CH, Huganir RL, Zou S, Lindsten T, Thompson CB, Mito T, Traystman RJ, Larsen T, Griffin DE, Mandir AS, Dawson TM, Dike S, Sappington AL, Kerr DA, Jonas EA, Kaczmarek LK, Hardwick JM. BAK Alters Neuronal Excitability and Can Switch from Anti- to Pro-Death Function during Postnatal Development. Developmental Cell 2003, 4: 575-585. PMID: 12689595, DOI: 10.1016/s1534-5807(03)00091-1.Peer-Reviewed Original ResearchMeSH KeywordsAge FactorsAnimalsAnimals, NewbornApoptosisBcl-2 Homologous Antagonist-Killer ProteinCentral Nervous SystemCentral Nervous System DiseasesCentral Nervous System Viral DiseasesDisease Models, AnimalEpilepsyExcitatory Postsynaptic PotentialsGenetic VectorsHippocampusKainic AcidMaleMembrane ProteinsMiceMice, KnockoutNeurodegenerative DiseasesNeuronsNeurotoxinsProtein Structure, TertiarySindbis VirusStrokeSynaptic TransmissionConceptsNeuronal excitabilityVirus infectionPostnatal developmentAlters neuronal excitabilityKainate-induced seizuresSpinal cord neuronsIschemia/strokeSindbis virus infectionNeuronal injuryCord neuronsNeuronal deathProtective effectSynaptic activityMouse modelParkinson's diseaseNeuron subtypesNeurotransmitter releasePro-death functionMiceNeuronsSpecific death stimuliDeathSeizuresPossible roleExcitability
1997
The Secretion of Classical and Peptide Cotransmitters from a Single Presynaptic Neuron Involves a Synaptobrevin-Like Molecule
Whim M, Niemann H, Kaczmarek L. The Secretion of Classical and Peptide Cotransmitters from a Single Presynaptic Neuron Involves a Synaptobrevin-Like Molecule. Journal Of Neuroscience 1997, 17: 2338-2347. PMID: 9065494, PMCID: PMC6573516, DOI: 10.1523/jneurosci.17-07-02338.1997.Peer-Reviewed Original ResearchMeSH KeywordsAcetylcholineAnimalsAplysiaCalciumCells, CulturedCoculture TechniquesElectric ConductivityGanglia, InvertebrateKineticsMagnesiumMembrane PotentialsMembrane ProteinsNerve Tissue ProteinsNeuronsNeurons, AfferentNeuropeptidesPatch-Clamp TechniquesPresynaptic TerminalsR-SNARE ProteinsRecombinant ProteinsSynapsesTetanus ToxinConceptsClassical transmittersSingle presynaptic neuronRelease of neuropeptidesSingle action potentialPresynaptic release sitesSecretion of peptidesNeuron B2Peptidergic synapsesSynaptic typesSensory neuronsPresynaptic neuronsTetanus toxinPeptide cotransmittersAction potentialsPresynaptic injectionSecretionNeuronsMolecular mechanismsSynapseTypes of transmittersB2CotransmitterNeuropeptidesPeptidesRelease
1993
The peptide FMRFa terminates a discharge in Aplysia bag cell neurons by modulating calcium, potassium, and chloride conductances
Fisher T, Lin C, Kaczmarek L. The peptide FMRFa terminates a discharge in Aplysia bag cell neurons by modulating calcium, potassium, and chloride conductances. Journal Of Neurophysiology 1993, 69: 2164-2173. PMID: 7688803, DOI: 10.1152/jn.1993.69.6.2164.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAplysiaCalcium ChannelsCells, CulturedChloride ChannelsElectric StimulationElectrophysiologyFMRFamideGangliaImmunohistochemistryIon ChannelsMembrane PotentialsMembrane ProteinsNeuritesNeuronsNeuropeptidesNeurotransmitter AgentsPotassium ChannelsStereotyped BehaviorTetradecanoylphorbol AcetateConceptsBag cell neuronsCell neuronsAction potentialsElectrical stimulationVoltage-activated calcium currentsOnset of afterdischargePowerful inhibitory influenceIntact abdominal gangliaIon substitution experimentsVoltage-clamp experimentsAfferent nervesProtein kinase C. 5Channel blockersCalcium currentPrimary cell culturesAbdominal ganglionInhibitory influenceAfterdischargesCyclic AMP analogueFMRFaOutward currentsNeuronal processesNeuronsAplysia bag cell neuronsReversal potential
1992
Structure and regulation of the MinK potassium channel
Blumenthal E, Kaczmarek L. Structure and regulation of the MinK potassium channel. Neurochemical Research 1992, 17: 869-876. PMID: 1407274, DOI: 10.1007/bf00993262.Peer-Reviewed Reviews, Practice Guidelines, Standards, and Consensus StatementsModulation by cAMP of a slowly activating potassium channel expressed in Xenopus oocytes
Blumenthal E, Kaczmarek L. Modulation by cAMP of a slowly activating potassium channel expressed in Xenopus oocytes. Journal Of Neuroscience 1992, 12: 290-296. PMID: 1370322, PMCID: PMC6575684, DOI: 10.1523/jneurosci.12-01-00290.1992.Peer-Reviewed Original ResearchMeSH Keywords8-Bromo Cyclic Adenosine MonophosphateAmino Acid SequenceAnimalsCell MembraneCyclic AMPFemaleGene ExpressionHumansMembrane PotentialsMembrane ProteinsMolecular Sequence DataMutagenesis, Site-DirectedOocytesPhosphorylationPotassium ChannelsPotassium Channels, Voltage-GatedProgesteroneProtein Kinase InhibitorsProtein KinasesRatsRNATransfectionXenopus laevisConceptsMinK proteinCAMP-dependent protein kinasePotential phosphorylation sitesXenopus oocytesCAMP levelsPhosphorylation sitesProtein kinasePlasma membraneKinase activityChannel proteinsIntracellular cAMP levelsProtein inhibitorProteinKinasePotassium channelsOocytesVoltage-dependent potassium currentsIsK
1991
Identification and localization of a dogfish homolog of human cystic fibrosis transmembrane conductance regulator.
Marshall J, Martin K, Picciotto M, Hockfield S, Nairn A, Kaczmarek L. Identification and localization of a dogfish homolog of human cystic fibrosis transmembrane conductance regulator. Journal Of Biological Chemistry 1991, 266: 22749-22754. PMID: 1718999, DOI: 10.1016/s0021-9258(18)54631-7.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBase SequenceCell MembraneCloning, MolecularCystic FibrosisCystic Fibrosis Transmembrane Conductance RegulatorDNADogfishHumansImmunoenzyme TechniquesMembrane ProteinsMolecular Sequence DataMolecular WeightProtein KinasesRectumSebaceous GlandsSequence Homology, Nucleic AcidSubstrate SpecificityConceptsCystic fibrosis transmembrane conductance regulatorHuman cystic fibrosis transmembrane conductance regulatorFibrosis transmembrane conductance regulatorTransmembrane conductance regulatorDogfish proteinRectal glandConductance regulatorPutative substrate sitesCyclic AMP-dependent protein kinaseAMP-dependent protein kinaseMajor phosphorylation siteCyclic AMP-dependent protein phosphorylationApical plasma membraneAmino acid sequenceStudy of regulationPhosphorylation sitesProtein phosphorylationCDNA clonesProtein kinaseSimilar molecular massCFTR sequencePlasma membraneAcid sequenceImmunolocalization studiesMolecular massPhosphorylation of membrane‐associated proteins by phorbol esters in isolated bag cell neurons of Aplysia
Azhderian E, Kaczmarek L. Phosphorylation of membrane‐associated proteins by phorbol esters in isolated bag cell neurons of Aplysia. Developmental Neurobiology 1991, 22: 105-115. PMID: 2030336, DOI: 10.1002/neu.480220202.Peer-Reviewed Original ResearchConceptsProtein kinase CBag cell neuronsKinase CPlasma membrane-containing fractionsProtein kinase C inhibitor H7Membrane-associated proteinsPhorbol esterExtent of phosphorylationMembrane-containing fractionsCell neuronsMembrane proteinsProtein phosphorylationNew speciesPhosphorylation statePlasma membraneTetradecanoyl phorbol 13Inhibitor H7Inactive phorbol esterIntact cellsPhosphate incorporationProtein extractsPhosphoproteinExtracellular mediumPhosphorylationProtein
1990
Cloning and expression of cDNA and genomic clones encoding three delayed rectifier potassium channels in rat brain
Swanson R, Marshall J, Smith J, Williams J, Boyle M, Folander K, Luneau C, Antanavage J, Oliva C, Buhrow S, Bennet C, Stein R, Kaczmarek L. Cloning and expression of cDNA and genomic clones encoding three delayed rectifier potassium channels in rat brain. Neuron 1990, 4: 929-939. PMID: 2361015, DOI: 10.1016/0896-6273(90)90146-7.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBase SequenceBrainCloning, MolecularDNAFemaleMembrane ProteinsMolecular Sequence DataOligonucleotide ProbesOocytesOrgan SpecificityPotassium ChannelsProtein BiosynthesisRatsRats, Inbred StrainsRestriction MappingRNA, MessengerSequence Homology, Nucleic AcidTranscription, GeneticXenopus
1982
Intracellular modulation of membrane channels by cyclic AMP-mediated protein phosphorylation in peptidergic neurons of Aplysia.
Strumwasser F, Kaczmarek L, Jennings K. Intracellular modulation of membrane channels by cyclic AMP-mediated protein phosphorylation in peptidergic neurons of Aplysia. The FASEB Journal 1982, 41: 2933-9. PMID: 6292000.Peer-Reviewed Reviews, Practice Guidelines, Standards, and Consensus StatementsConceptsProtein phosphorylationCyclic AMPPotassium channelsBag cell neuronsEgg-laying hormoneMembrane channelsIntracellular modulationPhosphorylationPeptidergic bag cell neuronsCell neuronsExact identityPeptidergic neuronsImportant componentControl eggsElectrical afterdischargeNeuroactive peptidesAMPEggsCorrelated behaviorNeuronsAplysiaPeptides