2001
Regulation of cyclin-dependent kinase 5 and casein kinase 1 by metabotropic glutamate receptors
Liu F, Ma X, Ule J, Bibb J, Nishi A, DeMaggio A, Yan Z, Nairn A, Greengard P. Regulation of cyclin-dependent kinase 5 and casein kinase 1 by metabotropic glutamate receptors. Proceedings Of The National Academy Of Sciences Of The United States Of America 2001, 98: 11062-11068. PMID: 11572969, PMCID: PMC58683, DOI: 10.1073/pnas.191353898.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCalcium ChannelsCasein KinasesCyclin-Dependent Kinase 5Cyclin-Dependent KinasesDopamine and cAMP-Regulated Phosphoprotein 32Enzyme InhibitorsIn Vitro TechniquesKineticsMaleMembrane PotentialsMethoxyhydroxyphenylglycolMiceMice, Inbred C57BLNeostriatumNerve Tissue ProteinsNeuronsPatch-Clamp TechniquesPhosphoproteinsPhosphorylationPhosphoserinePhosphothreonineProtein KinasesReceptors, Metabotropic GlutamateConceptsCasein kinase 1Cyclin-dependent kinase 5Ser-137Thr-75CK1 activityKinase 1Kinase 5DARPP-32Regulation of Cdk5Neuronal protein kinaseActivation of Cdk5Cellular functionsProtein kinaseDNA repairEnhanced phosphorylationFirst messengersCdk5 activitySpecific inhibitorCdk5Effects of DHPGMetabotropic glutamate receptorsNeurite outgrowthIC261Glutamate receptorsDHPG-induced increase
2000
Novel compounds, ‘1,3-selenazine derivatives’ as specific inhibitors of eukaryotic elongation factor-2 kinase
Cho S, Koketsu M, Ishihara H, Matsushita M, Nairn A, Fukazawa H, Uehara Y. Novel compounds, ‘1,3-selenazine derivatives’ as specific inhibitors of eukaryotic elongation factor-2 kinase. Biochimica Et Biophysica Acta 2000, 1475: 207-215. PMID: 10913818, DOI: 10.1016/s0304-4165(00)00061-1.Peer-Reviewed Original ResearchConceptsV-src-transformed NIH3T3 cellsEukaryotic elongation factor 2 kinaseProtein kinase AElongation factor 2 kinaseProtein kinase CProtein tyrosine kinasesEEF-2KProtein kinaseEEF-2K inhibitorNIH3T3 cellsCalmodulin-dependent protein kinaseV-Src kinaseMultiple protein kinasesCalmodulin-dependent protein kinase IIProtein levelsK inhibitorsProtein kinase IIEEF-2K.Kinase AKinase IITyrosine kinaseKinase CKinaseTs-4Specific inhibitor
1997
The Cytoplasmic Domain of Alzheimer’s Amyloid Precursor Protein Is Phosphorylated at Thr654, Ser655, and Thr668 in Adult Rat Brain and Cultured Cells
Oishi M, Nairn A, Czernik A, Lim G, Isohara T, Gandy S, Greengard P, Suzuki T. The Cytoplasmic Domain of Alzheimer’s Amyloid Precursor Protein Is Phosphorylated at Thr654, Ser655, and Thr668 in Adult Rat Brain and Cultured Cells. Molecular Medicine 1997, 3: 111-123. PMID: 9085254, PMCID: PMC2230054, DOI: 10.1007/bf03401803.Peer-Reviewed Original ResearchConceptsAlzheimer's disease amyloid precursor proteinCytoplasmic domainCultured cell linesCell cycle-dependent mannerAmyloid precursor proteinCultured cellsCycle-dependent mannerPhosphorylation state-specific antibodiesPhosphorylation-specific antibodiesPrecursor proteinCell linesProtein kinase C.Stoichiometric phosphorylationG2/M phaseAPP isoformsThr654Alzheimer amyloid precursor proteinOkadaic acidBiological functionsCell cycleKinase C.Intact cellsPhosphorylationHeLa cellsSpecific inhibitor