2009
Cytisine-Based Nicotinic Partial Agonists as Novel Antidepressant Compounds
Mineur YS, Eibl C, Young G, Kochevar C, Papke RL, Gündisch D, Picciotto MR. Cytisine-Based Nicotinic Partial Agonists as Novel Antidepressant Compounds. Journal Of Pharmacology And Experimental Therapeutics 2009, 329: 377-386. PMID: 19164465, PMCID: PMC2670591, DOI: 10.1124/jpet.108.149609.Peer-Reviewed Original ResearchMeSH KeywordsAlkaloidsAnimalsAntidepressive AgentsAzocinesCloning, MolecularData Interpretation, StatisticalElectrophysiologyEnvironmentFeeding BehaviorHindlimb SuspensionLaburnumMaleMiceMice, Inbred C57BLMotor ActivityNicotinic AgonistsOocytesPatch-Clamp TechniquesQuinolizinesReceptors, CholinergicSwimmingXenopus laevisConceptsAntidepressant-like effectsAntidepressant-like propertiesNicotinic partial agonistPartial agonistAntidepressant efficacyDose-dependent antidepressant-like effectNovelty-suppressed feeding testC57/BL6 miceBeta2 nAChRsAntidepressant-like activityTail suspension testBlood-brain barrierSelective partial agonistNicotinic acetylcholine receptorsNovel antidepressantsDevelopment of drugsBL6 miceAlpha3/beta4Alpha7 nAChRsAgonist effectsMood disordersRodent modelsSuspension testTail suspensionMouse model
2003
Identification and Characterization of AplysiaAdducin, an Aplysia Cytoskeletal Protein Homologous to Mammalian Adducins: Increased Phosphorylation at a Protein Kinase C Consensus Site during Long-Term Synaptic Facilitation
Gruenbaum LM, Gilligan DM, Picciotto MR, Marinesco S, Carew TJ. Identification and Characterization of AplysiaAdducin, an Aplysia Cytoskeletal Protein Homologous to Mammalian Adducins: Increased Phosphorylation at a Protein Kinase C Consensus Site during Long-Term Synaptic Facilitation. Journal Of Neuroscience 2003, 23: 2675-2685. PMID: 12684453, PMCID: PMC6742073, DOI: 10.1523/jneurosci.23-07-02675.2003.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsAplysiaCalmodulin-Binding ProteinsCloning, MolecularConsensus SequenceCytoskeletal ProteinsHumansKineticsMammalsMiceModels, BiologicalMolecular Sequence DataMotor NeuronsNervous SystemNeuronal PlasticityNeuronsNeurons, AfferentPhosphorylationProtein Kinase CProtein Structure, TertiarySequence Homology, Amino AcidSerotoninSynaptic TransmissionConceptsMammalian adducinsProtein kinase CProtein kinase C consensus sitesLong-term facilitationPKC phosphorylation sitesAplysia nervous systemProtein HomologousPhosphorylation sitesConsensus sitesMembrane cytoskeletonRegulatory componentsCandidate proteinsLong-term synaptic facilitationKinase CAdducinAplysia homologIncreased phosphorylationPhosphorylationNervous system extractsAplysia neuronsShort-term facilitationParticulate fractionSynaptic alterationsMotor neuronsSynaptic transmission
2001
Galanin receptor 1 gene expression is regulated by cyclic AMP through a CREB‐dependent mechanism
Zachariou V, Georgescu D, Kansal L, Merriam P, Picciotto M. Galanin receptor 1 gene expression is regulated by cyclic AMP through a CREB‐dependent mechanism. Journal Of Neurochemistry 2001, 76: 191-200. PMID: 11145992, DOI: 10.1046/j.1471-4159.2001.00018.x.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBase SequenceCell LineCloning, MolecularCodon, InitiatorColforsinCyclic AMPCyclic AMP Response Element-Binding ProteinGene Expression RegulationMiceMolecular Sequence DataMutagenesis, Site-DirectedNerve Growth FactorNeuronsPromoter Regions, GeneticReceptors, GalaninReceptors, NeuropeptideRegulatory Sequences, Nucleic AcidSequence Homology, Nucleic AcidTetradecanoylphorbol AcetateTransfectionConceptsLocus coeruleusOpiate withdrawalGalanin binding sitesPeripheral nervous systemCREB-dependent mechanismG protein-coupled receptorsLevels of cAMPProtein-coupled receptorsOpiate analgesiaNeuropeptide galaninGalanin receptorsGalR1 mRNANervous systemPlace preferenceTranscription factor CREBForskolin effectGALR1 expressionGalR1 geneCAMP levelsCyclic AMPCell linesBasal activityCRE-like siteTransient transfection assaysReceptors
1993
Calcium/calmodulin-dependent protein kinase I. cDNA cloning and identification of autophosphorylation site.
Picciotto MR, Czernik AJ, Nairn AC. Calcium/calmodulin-dependent protein kinase I. cDNA cloning and identification of autophosphorylation site. Journal Of Biological Chemistry 1993, 268: 26512-26521. PMID: 8253780, DOI: 10.1016/s0021-9258(19)74343-9.Peer-Reviewed Original ResearchMeSH KeywordsAdrenal GlandsAmino Acid SequenceAnimalsBase SequenceBinding SitesBrainCalcium-Calmodulin-Dependent Protein Kinase Type 1Calcium-Calmodulin-Dependent Protein KinasesCattleCloning, MolecularDNA, ComplementaryEscherichia coliLiverLungMolecular Sequence DataPhosphorylationRatsRNA, MessengerSequence Homology, Amino AcidConceptsCaM kinase IKinase IProtein kinaseCatalytic domainThreonyl residuesFusion proteinGlutathione S-transferase fusion proteinS-transferase fusion proteinCAMP-dependent protein kinaseDependent protein kinase IComplete amino acid sequenceBovine brain cDNA libraryInvariant amino acidsAmino acidsSynapsin IAmino acid sequenceBrain cDNA libraryClass of enzymesSynaptic vesicle proteinsProtein kinase ICaM kinase IIAutophosphorylation sitesRNase protection assaysSingle geneCDNA library
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 mass
1985
Aplysia neurons express a gene encoding multiple FMRFamide neuropeptides
Schaefer M, Picciotto M, Kreiner T, Kaldany R, Taussig R, Scheller R. Aplysia neurons express a gene encoding multiple FMRFamide neuropeptides. Cell 1985, 41: 457-467. PMID: 3838698, DOI: 10.1016/s0092-8674(85)80019-2.Peer-Reviewed Original ResearchConceptsAlternate RNA splicingAplysia nervous systemLys-Arg residuesHaploid genomeFMRFamide neuropeptidesRNA splicingCDNA clonesAnimal kingdomCDNA libraryMultiple transcriptsSingle copyCarboxy terminusAmino terminusInvertebrate tissuesFMRFamide peptidesDifferent tissuesPrecursor proteinPeptide Phe-MetGenesTerminusAplysia neuronsResiduesPhe-MetVariety of effectsArg-Phe