2001
Elongation Factor-2 Phosphorylation and the Regulation of Protein Synthesis by Calcium
Nairn A, Matsushita M, Nastiuk K, Horiuchi A, Mitsui K, Shimizu Y, Palfrey H. Elongation Factor-2 Phosphorylation and the Regulation of Protein Synthesis by Calcium. Progress In Molecular And Subcellular Biology 2001, 27: 91-129. PMID: 11575162, DOI: 10.1007/978-3-662-09889-9_4.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsCalciumCalcium-Calmodulin-Dependent Protein KinasesCell CycleCell DivisionCyclic AMP-Dependent Protein KinasesCysteine EndopeptidasesElongation Factor 2 KinaseHumansMolecular Sequence DataMultienzyme ComplexesNeuronsPeptide Chain Elongation, TranslationalPeptide Elongation Factor 2PhosphorylationProteasome Endopeptidase ComplexProtein BiosynthesisSequence Homology, Amino AcidSignal TransductionUbiquitinConceptsProtein synthesisElongation factor 2 phosphorylationDephosphorylation of eEF2Eukaryotic protein synthesisAminoacyl-tRNA synthetasesFactor 2 phosphorylationElongation factor 2Ribosomal proteinsRegulated processInitiation factorsDependent kinasesKey proteinsRate of elongationPeptidyl-tRNAPhysiological roleKinasePhosphorylationFactor 2EEF2P siteThr56ProteinSynthetasesDephosphorylationRibosomes
1997
Cell cycle-dependent phosphorylation of mammalian protein phosphatase 1 by cdc2 kinase
Kwon Y, Lee S, Choi Y, Greengard P, Nairn A. Cell cycle-dependent phosphorylation of mammalian protein phosphatase 1 by cdc2 kinase. Proceedings Of The National Academy Of Sciences Of The United States Of America 1997, 94: 2168-2173. PMID: 9122166, PMCID: PMC20059, DOI: 10.1073/pnas.94.6.2168.Peer-Reviewed Original ResearchConceptsProtein phosphatase 1PP-1Phosphatase 1Cdc2 kinaseMammalian protein phosphatase 1Cell cycle-dependent phosphorylationCyclin-dependent protein kinase inhibitorEukaryotic cell cycle progressionCell synchronization studiesIntact mammalian cellsNormal cell divisionPP-1 activityCell fractionation studiesState of phosphorylationProtein kinase inhibitorsCell cycle progressionMammalian cellsCell divisionThr-320Cycle progressionMitotic cellsT320NIH 3T3PhosphorylationFractionation studies
1995
Rapamycin inhibits ribosomal protein synthesis and induces G1 prolongation in mitogen-activated T lymphocytes.
Terada N, Takase K, Papst P, Nairn A, Gelfand E. Rapamycin inhibits ribosomal protein synthesis and induces G1 prolongation in mitogen-activated T lymphocytes. The Journal Of Immunology 1995, 155: 3418-26. PMID: 7561036, DOI: 10.4049/jimmunol.155.7.3418.Peer-Reviewed Original ResearchConceptsCell cycle progressionRibosomal protein mRNAsCycle progressionG2/M phaseRibosomal proteinsProtein synthesisProtein mRNAG1 prolongationCell cycleS phaseRibosomal protein mRNA translationRibosomal protein synthesisM phaseTotal cellular proteinEffect of rapamycinDNA synthesisNumber of ribosomesCell sizeCellular proteinsMRNA translation