1999
Protein phosphatase 1 modulation of neostriatal AMPA channels: regulation by DARPP–32 and spinophilin
Yan Z, Hsieh–Wilson L, Feng J, Tomizawa K, Allen P, Fienberg A, Nairn A, Greengard P. Protein phosphatase 1 modulation of neostriatal AMPA channels: regulation by DARPP–32 and spinophilin. Nature Neuroscience 1999, 2: 13-17. PMID: 10195174, DOI: 10.1038/4516.Peer-Reviewed Original ResearchConceptsPP-1Protein phosphatase 1DARPP-32Distinct molecular mechanismsPhosphatase 1Molecular mechanismsAMPA receptor-mediated synaptic transmissionPostsynaptic densityAMPA channelsRegulationSynaptic plasticitySpinophilinNeostriatal neuronsPlasticityPhysiological evidenceGlutamate channelsSynaptic transmissionAMPA receptorsPhosphoproteinProteinMechanismBindingActivityModulationCatalytic activity
1992
The role of protein phosphatases in synaptic transmission, plasticity and neuronal development
Nairn A, Shenolikar S. The role of protein phosphatases in synaptic transmission, plasticity and neuronal development. Current Opinion In Neurobiology 1992, 2: 296-301. PMID: 1322750, DOI: 10.1016/0959-4388(92)90118-5.Peer-Reviewed Original ResearchConceptsNeuronal developmentSerine/threonineRole of proteinsProtein phosphataseProtein dephosphorylationMolecular cloningTyrosine proteinIon channelsNervous systemPast year significant advancesNeuronal functionNeurotransmitter receptorsSpecific neuronsProteinSelective inhibitorEnzymeYears significant advancesSynaptic transmissionDephosphorylationCloningThreonineRolePhosphataseRegulationPlasticity
1989
Role of protein phosphorylation in neuronal signal transduction1
Hemmings H, Nairn A, McGuinness T, Huganir R, Greengard P. Role of protein phosphorylation in neuronal signal transduction1. The FASEB Journal 1989, 3: 1583-1592. PMID: 2493406, DOI: 10.1096/fasebj.3.5.2493406.Peer-Reviewed Original ResearchConceptsProtein phosphorylationSubstrate proteinsSignal transductionProtein kinaseMolecular mechanismsProtein phosphatase inhibitorSignal transduction processesPrecise molecular mechanismsAdditional molecular mechanismsSignal transduction1Extracellular signalsPhosphatase inhibitorAdditional phosphoproteinsPhysiological processesTransduction processesNicotinic acetylcholine receptorsPhosphorylationSynaptic transmissionNervous systemSynapsin IExcitable cellsDARPP-32TransductionKinaseNeurotransmitter release
1986
cGMP-dependent protein kinase enhances Ca2+ current and potentiates the serotonin-induced Ca2+ current increase in snail neurones
Paupardin-Tritsch D, Hammond C, Gerschenfeld H, Nairn A, Greengard P. cGMP-dependent protein kinase enhances Ca2+ current and potentiates the serotonin-induced Ca2+ current increase in snail neurones. Nature 1986, 323: 812-814. PMID: 3022154, DOI: 10.1038/323812a0.Peer-Reviewed Original ResearchConceptsIntracellular injectionCyclic GMP-dependent protein kinaseNeuronal membrane permeabilityAbsence of serotoninProtein kinaseSynaptic transmissionNeuronal functionIncrease of Ca2NeuronesCGMP-dependent protein kinaseGMP-dependent protein kinaseSerotoninSnail neuronesCyclic AMPMembrane permeabilityInjectionPhysiological roleProtein phosphorylationCa2CGMPKinase