2019
Molecular constituents and localization of the ionotropic GABA receptor complex in vivo
Tomita S. Molecular constituents and localization of the ionotropic GABA receptor complex in vivo. Current Opinion In Neurobiology 2019, 57: 81-86. PMID: 30784980, PMCID: PMC6629498, DOI: 10.1016/j.conb.2019.01.017.Peer-Reviewed Original ResearchConceptsNative receptor complexReceptor complexPore-forming subunitMolecular constituentsNew mechanistic insightsProtein familySubunit assemblyMajor molecular constituentsProperties of GABASynaptic localizationIonotropic GABA receptorsPrimary neuronsMechanistic insightsGABA receptor complexNative GABAReceptor regulationGABA receptorsNeuroligin-2R complexesGABAFast inhibitionPharmacological propertiesComplexesLocalizationSubunits
2009
Palmitoylation of Nicotinic Acetylcholine Receptors
Alexander JK, Govind AP, Drisdel RC, Blanton MP, Vallejo Y, Lam TT, Green WN. Palmitoylation of Nicotinic Acetylcholine Receptors. Journal Of Molecular Neuroscience 2009, 40: 12-20. PMID: 19693711, PMCID: PMC3523180, DOI: 10.1007/s12031-009-9246-z.Peer-Reviewed Original ResearchMeSH KeywordsAcetylcholineAcylationalpha7 Nicotinic Acetylcholine ReceptorAnimalsBinding SitesBiological AssayBrainCell LineElectric OrganHumansLigandsLipoylationMass SpectrometryNeuromuscular JunctionProtein Processing, Post-TranslationalProtein SubunitsProtein TransportReceptors, NicotinicSynaptic TransmissionTorpedoConceptsNicotinic acetylcholine receptorsSites of palmitoylationLigand-gated ion channelsDifferent posttranslational modificationsDisulfide bond formationMass spectrometry strategyLigand binding siteLow abundant proteinsAcetylcholine receptorsProtein palmitoylationPosttranslational modificationsSubunit assemblyPalmitoylationAbundant proteinsMuscle-type nAChRsIon channelsLoss of ligandBinding sitesSubunitsSitesReceptorsPhosphorylationTraffickingGlycosylationSensitive assay
2005
Biochemical characterization of the native Kv2.1 potassium channel
Chung J, Li M. Biochemical characterization of the native Kv2.1 potassium channel. The FEBS Journal 2005, 272: 3743-3755. PMID: 16008572, DOI: 10.1111/j.1742-4658.2005.04802.x.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsCell LineChromatography, AffinityChromatography, GelHumansMolecular Sequence DataPotassium Channels, Voltage-GatedProsencephalonProtein BindingProteomicsRatsRats, Sprague-DawleyShab Potassium ChannelsSolubilitySpectrometry, Mass, Matrix-Assisted Laser Desorption-IonizationConceptsBiochemical characterizationChannel complexLarge macromolecular complexesPotassium channelsPore-forming subunitRecombinant cell linesEukaryotic cellsPore complexFunctional diversityPosttranslational regulationKv2.2 subunitsSubunit assemblyVariety of tissuesMacromolecular complexesKv2.1 potassium channelOligomeric sizeNative polypeptideExpression cloningNative rat brainPhysiological relevanceRectifier potassium channelGel filtration chromatographySubunitsMRNA distributionModulatory subunit
1996
A mammalian gene with introns instead of exons generating stable RNA products
Tycowski K, Shu M, Steitz J. A mammalian gene with introns instead of exons generating stable RNA products. Nature 1996, 379: 464-466. PMID: 8559254, DOI: 10.1038/379464a0.Peer-Reviewed Original ResearchConceptsProtein-coding genesRibosomal subunit assemblyRibosomal RNA transcriptionSmall nucleolar RNAsMammalian genesSnoRNA genesEukaryotic cellsProtein codingMature rRNANucleolar RNAsHost genesSubunit assemblyDifferent intronsRNA transcriptionRNA productsExtensive complementarityIntronsGenesSnoRNAsExonsRNARRNATranscriptionPolysomesMaturation1
1993
Molecular requirements for the cell-surface expression of multisubunit ion-transporting ATPases. Identification of protein domains that participate in Na,K-ATPase and H,K-ATPase subunit assembly
Gottardi CJ, Caplan MJ. Molecular requirements for the cell-surface expression of multisubunit ion-transporting ATPases. Identification of protein domains that participate in Na,K-ATPase and H,K-ATPase subunit assembly. Journal Of Biological Chemistry 1993, 268: 14342-14347. PMID: 8390991, DOI: 10.1016/s0021-9258(19)85246-8.Peer-Reviewed Original ResearchConceptsK-ATPase alpha subunitK-ATPase beta subunitAlpha subunitBeta subunitCell surface expressionTerminal halfK-ATPaseCell surface deliveryEfficient cell surface expressionK-ATPase alphaNH2-terminal halfCOS-1 cellsIon-transporting ATPasesProtein domainsK-ATPase enzymeSubunit assemblySurface deliveryIntracellular vesiclesSubunit chimerasIndividual subunitsActive enzymeMolecular requirementsSubunitsCell surfaceBeta protein
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