1997
A molecular modeling analysis of the binding interactions between the okadaic acid class of natural product inhibitors and the ser-thr phosphatases, PP1 and PP2A
Gauss C, Sheppeck J, Nairn A, Chamberlin R. A molecular modeling analysis of the binding interactions between the okadaic acid class of natural product inhibitors and the ser-thr phosphatases, PP1 and PP2A. Bioorganic & Medicinal Chemistry 1997, 5: 1751-1773. PMID: 9354231, DOI: 10.1016/s0968-0896(97)00145-4.Peer-Reviewed Original ResearchConceptsSerine-threonine proteinOkadaic acid classSignal transduction pathwaysNatural product inhibitorsCatalytic subunitTransduction pathwaysPP1Endogenous substratesProduct inhibitorsMolecular modeling analysisSer-ThrAcid classPP2AImportant roleComputer-generated modelsInhibitorsSubunitsProteinPathway
1993
Phosphorylation of elongation factor 2 in normal and malignant rat glial cells.
Bagaglio DM, Cheng EH, Gorelick FS, Mitsui K, Nairn AC, Hait WN. Phosphorylation of elongation factor 2 in normal and malignant rat glial cells. Cancer Research 1993, 53: 2260-4. PMID: 8485712.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCalciumCalcium-Calmodulin-Dependent Protein KinasesCalmodulinCell DivisionCells, CulturedElongation Factor 2 KinaseGliomaMaleNeurogliaPeptide Elongation Factor 2Peptide Elongation FactorsPhosphorylationPrecipitin TestsProtein KinasesRatsRats, Sprague-DawleyTrifluoperazineTumor Cells, CulturedConceptsRat brain white matterNormal glial tissueGlial tissueGlioma cellsC6 cellsC6 rat glioma cellsCaM kinase IIIRat glial cellsFactor 2Rat glioma cellsBrain white matterNormal gliaElongation factor 2Glial cellsRat brainWhite matterTumor tissueBasal levelsIII activityCellular proliferationTissueDependent proteinsCellsEndogenous substratesHomogenates