2011
Beyond the Dopamine Receptor: Regulation and Roles of Serine/Threonine Protein Phosphatases
Walaas SI, Hemmings HC, Greengard P, Nairn AC. Beyond the Dopamine Receptor: Regulation and Roles of Serine/Threonine Protein Phosphatases. Frontiers In Neuroanatomy 2011, 5: 50. PMID: 21904525, PMCID: PMC3162284, DOI: 10.3389/fnana.2011.00050.Peer-Reviewed Original ResearchSerine/threonine proteinARPP-16Signaling pathwaysDARPP-32Striatal signaling pathwaysRegulator of calmodulinMultiple neurological diseasesNovel roleMolecular actionsProteinPP1Monophosphate-regulated phosphoproteinPhosphoproteinMolecular integratorPleiotropic actionsMultiple stepsMajor subclassesDopamine receptorsPathwayHuntington's diseaseRecent studiesStriatal signalingPP2ACentral nervous systemPP2B
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
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