1999
The design, synthesis, and biological evaluation of analogues of the serine-threonine protein phosphatase 1 and 2A selective inhibitor microcystin LA: rational modifications imparting PP1 selectivity
Aggen J, Humphrey J, Gauss C, Huang H, Nairn A, Chamberlin A. The design, synthesis, and biological evaluation of analogues of the serine-threonine protein phosphatase 1 and 2A selective inhibitor microcystin LA: rational modifications imparting PP1 selectivity. Bioorganic & Medicinal Chemistry 1999, 7: 543-564. PMID: 10220039, DOI: 10.1016/s0968-0896(98)00254-5.Peer-Reviewed Original ResearchConceptsPP1 selectivityProtein phosphatase 1Serine-threonine proteinMicrocystin-LAFirst-generation analogsSmall molecule inhibitorsPhosphatase 1Observed selectivityBiological evaluationMolecular modeling analysisMolecule inhibitorsRational modificationSelectivityStructural modificationsSynthesisAnaloguesInhibition assaysPP1MicrocystinsProteinLaModificationAssaysInhibitors
1994
Correlation between protein kinase C binding proteins and substrates in REF52 cells.
Hyatt S, Liao L, Aderem A, Nairn A, Jaken S. Correlation between protein kinase C binding proteins and substrates in REF52 cells. Molecular Cancer Research 1994, 5: 495-502. PMID: 8049156.Peer-Reviewed Original ResearchMeSH KeywordsBlotting, WesternCalmodulin-Binding ProteinsCell LineCell Line, TransformedCell Transformation, NeoplasticDown-RegulationIntracellular Signaling Peptides and ProteinsIsoenzymesMembrane ProteinsMolecular WeightMyristoylated Alanine-Rich C Kinase SubstratePhosphatidylserinesPhosphorylationProtein BindingProtein DenaturationProtein Kinase CProtein Kinase C-alphaProteinsSolubilityConceptsProtein kinase CREF52 cellsPKC substrateKinase CBinding proteinProperties of PKCCalmodulin-Sepharose chromatographyBlot overlay assaysProteins/substratesMajor PKC substrateMajor binding proteinPhosphorylation assaysBlot overlayOverlay assaysTarget proteinsBasal phosphorylationProteinCellsSufficient affinityMARCKSAssaysPhosphorylationSubstratePhenotypeSV40
1991
Evidence for isoproterenol-induced phosphorylation of phosphatase inhibitor-1 in the intact heart.
Neumann J, Gupta R, Schmitz W, Scholz H, Nairn A, Watanabe A. Evidence for isoproterenol-induced phosphorylation of phosphatase inhibitor-1 in the intact heart. Circulation Research 1991, 69: 1450-1457. PMID: 1659500, DOI: 10.1161/01.res.69.6.1450.Peer-Reviewed Original ResearchConceptsPhosphatase inhibitor-1Protein phosphatase inhibitor-1Type 1 phosphatase activityPhosphatase activityInhibitor-1Sodium dodecyl sulfate gelsDodecyl sulfate gelsIsoproterenol-induced phosphorylationSulfate gelsProteinRadioactive proteinsPhosphorylationPmol 32P/KdPhysiological bufferAntiserumActivityIndirect assayConcentrations of isoproterenolAgonist isoproterenolActivationAssaysVivoIntact heartCAMP