1999
Use of knock-out mice to determine the molecular basis for the actions of nicotine
Picciotto M, Zoli M, Changeux J. Use of knock-out mice to determine the molecular basis for the actions of nicotine. Nicotine & Tobacco Research 1999, 1: s121-s125. PMID: 11768168, DOI: 10.1080/14622299050011931.Peer-Reviewed Original ResearchConceptsElectrophysiological propertiesBehavioral effectsSubunit combinationsAction of nicotineDifferent neurotransmitter systemsEffects of nicotineMesolimbic dopamine systemIndividual receptor subtypesNicotinic acetylcholine receptorsBinding of nicotinePossible subunit combinationsDifferent subunit combinationsNicotine effectsNicotine receptorsNicotine reinforcementReceptor subtypesDopamine levelsNeurotransmitter systemsDopamine systemNicotinic subunitsAcetylcholine receptorsAddictive propertiesNicotineMiceBeta2 subunit
1995
Abnormal avoidance learning in mice lacking functional high-affinity nicotine receptor in the brain
Picciotto M, Zoli M, Léna C, Bessis A, Lallemand Y, LeNovère N, Vincent P, Pich E, Brûlet P, Changeux J. Abnormal avoidance learning in mice lacking functional high-affinity nicotine receptor in the brain. Nature 1995, 374: 65-67. PMID: 7870173, DOI: 10.1038/374065a0.Peer-Reviewed Original ResearchConceptsHigh-affinity nicotine receptorsNeuronal nicotinic acetylcholine receptorsBrains of miceΒ2-/- miceNicotinic acetylcholine receptorsThalamic neuronsNicotine applicationFunctional nAChRsNicotine receptorsBrain slicesNicotinic subunitsAbnormal avoidanceAcetylcholine receptorsAspects of behaviorHigh-affinity binding sitesMutant miceElectrophysiological recordingsPassive avoidanceAssociative memoryMiceNicotineNeuronal nicotinic subunitsNon-mutant siblingsBrainReceptors
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