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
1994
Rapamycin selectively inhibits translation of mRNAs encoding elongation factors and ribosomal proteins.
Terada N, Patel H, Takase K, Kohno K, Nairn A, Gelfand E. Rapamycin selectively inhibits translation of mRNAs encoding elongation factors and ribosomal proteins. Proceedings Of The National Academy Of Sciences Of The United States Of America 1994, 91: 11477-11481. PMID: 7972087, PMCID: PMC45254, DOI: 10.1073/pnas.91.24.11477.Peer-Reviewed Original ResearchConceptsRibosomal proteinsElongation factorProtein synthesisRibosomal protein mRNAsRibosomal protein synthesisTranslation of mRNAsP70 S6 kinaseRibosomal S6 proteinElongation factor 2Higher eukaryotesNonribosomal proteinsPolysomal associationRate of biosynthesisTranslational regulationMammalian cellsMRNA translationS6 kinaseAddition of rapamycinS6 proteinSubsequent phosphorylationEEF-2Translational levelImmunosuppressant rapamycinQuiescent cellsSelective proteins
1987
Identification of the major Mr 100,000 substrate for calmodulin-dependent protein kinase III in mammalian cells as elongation factor-2.
Nairn A, Palfrey H. Identification of the major Mr 100,000 substrate for calmodulin-dependent protein kinase III in mammalian cells as elongation factor-2. Journal Of Biological Chemistry 1987, 262: 17299-17303. PMID: 3693353, DOI: 10.1016/s0021-9258(18)45377-x.Peer-Reviewed Original ResearchConceptsProtein kinase IIIElongation factor 2Kinase IIIMammalian cellsThreonine residuesCalmodulin-dependent protein kinase IIIDependent protein kinase IIIPhosphorylated EF-2Endogenous GTPase activityAmino acid sequencingSpecies of MrFactor 2Inhibits protein synthesisTryptic phosphopeptidesGTPase activityNucleic acid sequencingCytoplasmic localizationMajor substrateN-terminalPeptidyl-tRNATerminal sequenceSalt-washed ribosomesProtein synthesisEF-1Thr-Asp