2011
Random insertion of split-cans of the fluorescent protein venus into Shaker channels yields voltage sensitive probes with improved membrane localization in mammalian cells
Jin L, Baker B, Mealer R, Cohen L, Pieribone V, Pralle A, Hughes T. Random insertion of split-cans of the fluorescent protein venus into Shaker channels yields voltage sensitive probes with improved membrane localization in mammalian cells. Journal Of Neuroscience Methods 2011, 199: 1-9. PMID: 21497167, PMCID: PMC3281265, DOI: 10.1016/j.jneumeth.2011.03.028.Peer-Reviewed Original ResearchMeSH KeywordsBacterial ProteinsCell LineCell Line, TumorCell MembraneCytosolDNA Transposable ElementsFluorescent DyesHumansKidneyLuminescent ProteinsMembrane PotentialsMembrane ProteinsMicroscopy, ConfocalMicroscopy, FluorescenceModels, MolecularMutation, MissenseNeuroblastomaPatch-Clamp TechniquesPeptide FragmentsProtein FoldingProtein MultimerizationProtein Structure, SecondaryProtein Structure, TertiaryRecombinant Fusion ProteinsShaker Superfamily of Potassium ChannelsTransfectionConceptsShaker subunitsYellow fluorescent proteinEndoplasmic reticulumMammalian cellsNon-fluorescent halvesMisfolded monomersPlasma membrane expressionFluorescent protein VenusShaker potassium channelFluorescent protein (FP) voltage sensorsMembrane localizationPlasma membraneFluorescent proteinRandom insertionMembrane expressionSubunitsMembrane potentialIntracellular fluorescencePotassium channelsCellsFluorescent probeΔF/FVoltage sensorTetramerizationProtein
1999
Inhibition of neurotransmitter release in the lamprey reticulospinal synapse by antibody-mediated disruption of SNAP-25 function
Low P, Norlin T, Risinger C, Larhammar D, Pieribone V, Shupliakov O, Brodin L. Inhibition of neurotransmitter release in the lamprey reticulospinal synapse by antibody-mediated disruption of SNAP-25 function. European Journal Of Cell Biology 1999, 78: 787-793. PMID: 10604655, DOI: 10.1016/s0171-9335(99)80029-6.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAntibodies, MonoclonalAxonsCell MembraneImmunohistochemistryIn Situ HybridizationLampreysMembrane ProteinsMicroinjectionsMicroscopy, ElectronNerve Tissue ProteinsNeurotransmitter AgentsProtein BindingRecombinant Fusion ProteinsSpinal CordSynapsesSynaptic TransmissionSynaptic VesiclesSynaptosomal-Associated Protein 25ConceptsPlasma membraneSynaptic vesiclesSNAP-25Lamprey giant reticulospinal synapsePresynaptic plasma membraneSynaptic vesicle exocytosisLamprey reticulospinal synapseSNARE protein SNAP-25Protein SNAP-25Synaptic vesicle clustersNeurotransmitter releaseSNARE complexMolecular machineryVesicle exocytosisMembrane fusionVesicle cyclingPresynaptic microinjectionVesicle clustersSyntaxinPresynaptic membraneVesiclesElectron microscopic analysisAntibody-mediated disruptionMembraneMicroscopic analysis
1993
Evolutionary conservation of synaptosome-associated protein 25 kDa (SNAP-25) shown by Drosophila and Torpedo cDNA clones.
Risinger C, Blomqvist AG, Lundell I, Lambertsson A, Nässel D, Pieribone VA, Brodin L, Larhammar D. Evolutionary conservation of synaptosome-associated protein 25 kDa (SNAP-25) shown by Drosophila and Torpedo cDNA clones. Journal Of Biological Chemistry 1993, 268: 24408-24414. PMID: 8226991, DOI: 10.1016/s0021-9258(20)80540-7.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBase SequenceBiological EvolutionBlotting, NorthernConserved SequenceDNA, ComplementaryDrosophila melanogasterDrosophila ProteinsIn Situ HybridizationMembrane ProteinsMolecular Sequence DataNerve Tissue ProteinsSequence Homology, Amino AcidSynaptosomal-Associated Protein 25TorpedoConceptsVesicle dockingCDNA clonesMembrane fusionSNAP-25Basic molecular machineryDisplay sequence similarityMembrane-spanning regionSynaptic vesicle dockingDegree of conservationAmino acid identityRay Torpedo marmorataEvolutionary conservationTorpedo proteinDrosophila melanogasterMolecular machinerySequence similarityMembrane attachmentAcid identityNeuron-specific proteinCysteine residuesDrosophilaSynaptobrevinProtein 25Situ hybridizationProtein